Top 10 Biorxiv Papers Today in Cell Biology


2.547 Mikeys
#1. TurboID-mediated proximity labelling of cytoophidium proteome in Drosophila
Bo Zhang, Yuanbing Zhang, Ji-Long Liu
Proximity-based biotinylation combined with mass spectrometry has emerged as a powerful approach to study protein interaction networks and protein subcellular compartmentation. However, low kinetics and the requirement of toxic chemicals limit the broad utilisation of current proximity labelling methods in living organisms. TurboID, the newly engineered promiscuous ligase, has been reported to label bait proteins effectively in various species. Here, we systematically demonstrated the application of TurboID-mediated biotinylation in a wide range of developmental stages and tissues, and we also verified the feasibility of TurboID-mediated labelling in desired cells via cell-type-specific GAL4 driver in Drosophila. Furthermore, using TurboID-mediated biotinylation coupled with mass spectrometry, we characterized the proximate proteome of the cytoophidium, a newly identified filamentous structure containing the metabolic enzyme CTP synthase (CTPS) in Drosophila. Our study demonstrates a referable tool and resource for research in...
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biorxivpreprint: TurboID-mediated proximity labelling of cytoophidium proteome in Drosophila https://t.co/Ivc6BDJ3Bg #bioRxiv
biorxiv_cellbio: TurboID-mediated proximity labelling of cytoophidium proteome in Drosophila https://t.co/hzVAaGpqmW #biorxiv_cellbio
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2.145 Mikeys
#2. In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen
Danielle M Paul, Judith Mantell, Ufuk Borucu, Jennifer Coombs, Katherine J Surridge, John M Squire, Paul Verkade, Mark P Dodding
Microtubules and filamentous (F-) actin engage in complex interactions to drive many cellular processes from subcellular organisation to cell division and migration. This is thought to be largely controlled by proteins that interface between the two structurally distinct cytoskeletal components. Here, we use cryo-electron tomography to demonstrate that the microtubule lumen can be occupied by extended segments of F-actin in small-molecule induced, microtubule-based cellular projections. We uncover an unexpected versatility in cytoskeletal form that may prompt a significant development of our current models of cellular architecture and offer a new experimental approach for the in-situ study of microtubule structure and contents.
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eva_karasmanis: Some prefer actin, some microtubules, some think about actin-MT crosstalk.. but Actin *IN* microtubules?!?!? Paul, Mantell et al make their case with in situ #cryoEM 🤯 #cytoskeletonwars #cryoET https://t.co/rrcAblo5GG https://t.co/HF2n123Erd
PromPreprint: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/iPzvZ1lcwe
PavelTomancak: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
KGoepfrich: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
Po_Strale: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
BriegelAriane: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
andy_utoronto: RT @PromPreprint: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/iPzvZ1lcwe
KrisKilian: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
ScopeShifu: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
DrMCJones33: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
Jamie_Rossjohn: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
LashuelLab: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
harrietm11: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
SvobodaLab: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
sshekhr: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
builab: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
FKHM: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
t2438: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
CRBM_Montpel: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
LudingtonWill: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
RocksAnnaa: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
PhiloNeurosci: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
WUMIN_LAB: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
mshanj: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
feyzanar: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
DDaCrema1: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
armish1910: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
pituvilarnadal: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
ZelzerLab: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
brantmwebster: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
NicoBroguiere: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
Yoshi__Ichikawa: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
gracechao: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
MHVerlhac: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
Thehumbleartis1: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
dmborek: RT @cryoEM_Papers: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/fV0DM5458d
SamirKMaji1: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
FelipeIMerino: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
nsreelaja: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
MSYSN: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
alauld1: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
divergente81: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
ParrenoJustin: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
markocms: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
zcseresn: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
jijumon109: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
emoryici: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
KraussLab: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
maxferrin: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
Anneke_Sanders: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
MaxSchelski: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
key_carvalho: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
FerentJ: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
Tabdanov: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
LucaCirillo17: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
Childericks: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
Kamaleshkumari_: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
genehackerman44: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
FereshtehMemar2: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
AllinghamJohn: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
JethroEzra: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
DInoueMT: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
ME3T_Aachen: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
jmdelgado_: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
CastroLeha: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
INoordstra: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
EricTheveneau: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
cheesan_tong: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
PahmeierFelix: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
adayinthefly: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
Lcklemm: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
Sandeep44119670: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
AkivaAnat: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
devinasingh30: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
CorinneTovey: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
langridge_paul: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
AdiyantL: RT @biorxiv_cellbio: In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen https://t.co/sKxTXqH44J #bior…
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2.031 Mikeys
#3. Structural insights into filament recognition by cellular actin markers
Archana Kumari, Shubham Kesarwani, Manjunath G Javoor, Kutti R Vinothkumar, Minhaj Sirajuddin
Cellular studies of filamentous actin (F-actin) processes commonly utilize fluorescent versions of toxins, peptides and proteins that bind actin. While the choice of these markers has been largely based on availability and ease, there is a severe dearth of structural data for an informed judgment in employing suitable F-actin markers for a particular requirement. Here we describe the electron cryomicroscopy structures of phalloidin, lifeAct and utrophin bound to F-actin, providing the first high-resolution structures and comparison of widely used actin markers and their influence towards F-actin. Our results show that phalloidin binding does not induce conformations and lifeAct specifically recognizes ADP-actin state, which can be used as a sensor for distinguishing different nucleotide states of F-actin. The utrophin structural model aided designing minimal utrophin, which can be utilized as F-actin marker. Together, our study provides a structural perspective, where the binding sites of utrophin and lifeAct overlap with majority...
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christlet: Structural insights into filament recognition by cellular actin markers [NEW RESULTS] https://t.co/lY7hKQC9oY
cryoEM_Papers: Structural insights into filament recognition by cellular actin markers https://t.co/xANaB5cxRr
PromPreprint: Structural insights into filament recognition by cellular actin markers https://t.co/Q2ZLCMeESF
DeepakNModi: RT @biorxivpreprint: Structural insights into filament recognition by cellular actin markers https://t.co/fHRibwAAKn #bioRxiv
Roy_Lab_Thinks: RT @biorxivpreprint: Structural insights into filament recognition by cellular actin markers https://t.co/fHRibwAAKn #bioRxiv
Roswitamind: RT @christlet: Structural insights into filament recognition by cellular actin markers [NEW RESULTS] https://t.co/lY7hKQC9oY
MSYSN: RT @biorxivpreprint: Structural insights into filament recognition by cellular actin markers https://t.co/fHRibwAAKn #bioRxiv
trembleaudusart: RT @biorxivpreprint: Structural insights into filament recognition by cellular actin markers https://t.co/fHRibwAAKn #bioRxiv
JosephMathewK: RT @biorxivpreprint: Structural insights into filament recognition by cellular actin markers https://t.co/fHRibwAAKn #bioRxiv
baskarb11: RT @biorxivpreprint: Structural insights into filament recognition by cellular actin markers https://t.co/fHRibwAAKn #bioRxiv
RanabirNMR: RT @biorxivpreprint: Structural insights into filament recognition by cellular actin markers https://t.co/fHRibwAAKn #bioRxiv
Kamaleshkumari_: RT @biorxivpreprint: Structural insights into filament recognition by cellular actin markers https://t.co/fHRibwAAKn #bioRxiv
CaraMoravec: RT @biorxivpreprint: Structural insights into filament recognition by cellular actin markers https://t.co/fHRibwAAKn #bioRxiv
KonstantinosNa9: RT @christlet: Structural insights into filament recognition by cellular actin markers [NEW RESULTS] https://t.co/lY7hKQC9oY
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2.01 Mikeys
#4. Osmotic stress-induced, rapid clustering of IGF2BP proteins nucleates stress granule assembly
Wei-Jie Zeng, Chuxin Lu, Yuanyuan Shi, Xinxin Chen, Jie Yao
Stress granules (SGs) are formed in the cytoplasm by liquid-liquid phase separation (LLPS) of translationally-stalled mRNA and RNA-binding proteins during stress response. Understanding the mechanisms governing SG assembly requires imaging SG formation in real time. Here we used live cell imaging and super-resolution imaging to visualize SG assembly in human cells. We found that IGF2BP proteins formed microscopically visible clusters almost instantaneously upon osmotic stress, prior to the recruitment of G3BP1 and TIA1. The rapid clustering of IGF2BP1 was ATP-independent and was mediated by its KH3/4 di-domains and an intrinsically disordered region (IDR), whereas ATP depletion inhibited the recruitment of G3BP1 and TIA1. Moreover, we detected cytoplasmic clusters of IGF2BP1 below the optical resolution in normal cells and found IGF2BP1 forming a dense granule associated with multiple clusters of poly(A) mRNA in mature SGs. Thus, ATP-independent, rapid clustering of IGF2BP nucleates SG assembly during osmotic stress.
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biorxivpreprint: Osmotic stress-induced, rapid clustering of IGF2BP proteins nucleates stress granule assembly https://t.co/ndTOFX2X3u #bioRxiv
biorxiv_cellbio: Osmotic stress-induced, rapid clustering of IGF2BP proteins nucleates stress granule assembly https://t.co/PDJ9TTdf0T #biorxiv_cellbio
NZthRzXeiplAQA6: RT @biorxivpreprint: Osmotic stress-induced, rapid clustering of IGF2BP proteins nucleates stress granule assembly https://t.co/ndTOFX2X3u…
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2.009 Mikeys
#5. The transcriptomic response of cells to a drug combination is more than the sum of the responses to the monotherapies
Jennifer E. L. Diaz, Mehmet Eren Ahsen, Thomas Schaffter, Xintong Chen, Ronald B. Realubit, Charles Karan, Andrea Califano, Bojan Losic, Gustavo Stolovitzky
Our ability to predict the effects of drug combinations is limited, in part by limited understanding of how the transcriptional response of two monotherapies results in that of their combination. We performed the first analysis of matched time course RNAseq profiling of cells treated with both single drugs and their combinations. The transcriptional signature of the synergistic combination we studied had unique gene expression not seen in either constituent monotherapy. This can be explained mechanistically by the sequential activation of transcription factors in time in the gene regulatory network. The nature of this transcriptional cascade suggests that drug synergy may ensue when the transcriptional responses elicited by two unrelated individual drugs are correlated. We used these results as the basis of a simple prediction algorithm attaining an AUROC of 0.84 in the prediction of synergistic drug combinations in an independent dataset.
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biorxivpreprint: The transcriptomic response of cells to a drug combination is more than the sum of the responses to the monotherapies https://t.co/ga2RlkzR8e #bioRxiv
biorxiv_cellbio: The transcriptomic response of cells to a drug combination is more than the sum of the responses to the monotherapies https://t.co/7HwLqUwJgC #biorxiv_cellbio
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2.009 Mikeys
#6. Hepatocytic Prominin-1 protects liver fibrosis by stabilizing the SMAD7 protein
Hyun Lee, Dong-Min Yu, Min Jee Um, Seo Yeon Yoon, Ki-Tae Kim, Young Jae Kwon, Sungsoo Lee, Myeong-Seok Bahn, Ki Hoon Jung, Jae-Seon Lee, Young-Gyu Ko
Background and Aims: Prominin-1 (PROM1) is known to be upregulated in hepatocytic progenitor cells (HPCs) and cholangiocytes of fibrotic livers. To understand the function of upregulated PROM1 during liver fibrosis, we analyzed liver fibrosis from global and liver-specific Prom1 knockout mice and investigated the molecular mechanism of how Prom1 protects the liver against liver fibrosis. Methods: We analyzed PROM1 expression from human liver with mild and severe liver fibrosis (n=4-9). Liver fibrosis was induced by carbon tetrachloride (CCl4) treatment and bile duct ligation (BDL) from wild type and global and liver-specific knockout mice (n=3-13). The severity of liver fibrosis was determined by qRT-PCR, immunostaining and immunoblotting for fibrotic markers such as αSMA, collagen. TGFβ signaling was also analyzed from fibrotic liver and primary hepatocytes of wild type and global and liver-specific knockout mice (n=3-5). Molecular interaction between PROM1 and SMAD7 was determined by endogenous and exogenous...
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biorxivpreprint: Hepatocytic Prominin-1 protects liver fibrosis by stabilizing the SMAD7 protein https://t.co/mWxw35dC7N #bioRxiv
biorxiv_cellbio: Hepatocytic Prominin-1 protects liver fibrosis by stabilizing the SMAD7 protein https://t.co/qyuqQp4GfG #biorxiv_cellbio
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Total Words: 8431
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2.008 Mikeys
#7. Individual kinetochore-fibers locally dissipate force to maintain robust mammalian spindle structure
Alexandra F Long, Pooja Suresh, Sophie Dumont
At cell division, the mammalian kinetochore binds many spindle microtubules that make up the kinetochore-fiber. To segregate chromosomes, the kinetochore-fiber must be dynamic and generate and respond to force. Yet, how it remodels under force remains poorly understood. Kinetochore-fibers cannot be reconstituted in vitro, and exerting controlled forces in vivo remains challenging. Here, we use microneedles to pull on mammalian kinetochore-fibers and probe how sustained force regulates their dynamics and structure. We show that force lengthens kinetochore-fibers by persistently favoring plus-end polymerization, not by increasing polymerization rate. We demonstrate that force suppresses depolymerization at both plus- and minus-ends, rather than sliding microtubules within the kinetochore-fiber. Finally, we observe that kinetochore-fibers break but do not detach from kinetochores or poles. Together, this work suggests an engineering principle for spindle structural homeostasis: different physical mechanisms of local force dissipation...
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biorxivpreprint: Individual kinetochore-fibers locally dissipate force to maintain robust mammalian spindle structure https://t.co/XYvvtEGg5g #bioRxiv
biorxiv_cellbio: Individual kinetochore-fibers locally dissipate force to maintain robust mammalian spindle structure https://t.co/KpMGGs5KZL #biorxiv_cellbio
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1.998 Mikeys
#8. Robust lysosomal rewiring in Mtb infected macrophages mediated by Mtb lipids restricts the intracellular bacterial survival
Kuldeep Sachdeva, Manisha Goel, Malvika Sudhakar, Mansi Mehta, Rajmani Raju, Karthik Raman, Amit Singh, Varadharajan Sundaramurthy
Intracellular pathogens commonly manipulate the host lysosomal system for their survival, however whether this affects the organization and functioning of the endo-lysosomal system itself is not known. Here, we show using in vitro and in vivo infections that the lysosomal content and activity is globally elevated in M. tuberculosis infected macrophages. The enhanced lysosomal state is sustained over time and defines an adaptive homeostasis of the infected cell. Lysosomal alterations are caused by mycobacterial surface components, notably the cell wall lipid SL-1, which functions through the mTORC1-TFEB axis. Mtb mutant defective for SL-1 levels shows reduced lysosomal content and activity compared to wild type. Importantly, this phenotype is conserved during in vivo infection, as well as in clinical Mtb isolates that are deficient in SL-1. The alteration in lysosomal phenotype in mutant Mtb lead to decreased lysosomal delivery of Mtb, and importantly, increased survival of intracellular Mtb. These results define the global...
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Total Words: 17007
Unqiue Words: 3673

1.997 Mikeys
#9. Multi-Differentiation Potential Is Necessary For Optimal Tenogenesis Of Tendon Stem Cells
Ibtesam Rajpar, Jennifer G Barrett
Tendon injury is a significant clinical problem, and regenerative treatments are limited by our understanding of endogenous tendon stem cells. Recent evidence suggests that tendon stem cells are diverse in phenotypic character, and may in fact exist on a spectrum of differentiation capacities. However, the functional significance of each differentiation phenotype is poorly understood. Toward this end, we performed a comprehensive assessment of differentiation capacity toward four connective tissue lineages (adipose, bone, cartilage and tendon) with clonal tendon stem cell lines to: 1) evaluate the differences, if any, in tenogenic potential, and 2) identify the relationships in differentiation phenotype and proliferation capacity. Tendon stem cells were derived from whole equine flexor tendons for this study. Clonal tendon stem lines were generated by low-density cell plating, and subjected to standard assays of tri-lineage differentiation and population doublings. For tenogenesis, a previously engineered three-dimensional...
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Authors: 2
Total Words: 7876
Unqiue Words: 2811

1.997 Mikeys
#10. Alpha 6 Integrins Regulate the Expression of Laminin-511 and CXCR4 to Promote Endothelial Tubular Morphogenesis
Hao Xu, Kevin Pumiglia, Susan E LaFlamme
During angiogenesis, endothelial cells engage components of the extracellular matrix through integrin-mediated adhesion. Endothelial cells express laminin-411 and laminin-511 that bind to integrins, including the α6 integrins, α6β1 and α6β4. However, little is known about the contribution of these laminins to endothelial tubular morphogenesis and stability. We used two organotypic angiogenesis assays in conjunction with RNAi approaches to demonstrate that endothelial depletion of either the α4 chain of laminin-411 or the α5 chain of laminin-511 inhibited sprouting and tube formation. Depletion of α6 integrins resulted in similar phenotypes. Interestingly, depletion of α6 integrins also inhibited the expression of laminin-511, which correlated with the loss of tubular stability. Loss of either α6 integrins or laminin-511 resulted in the inhibition of the expression of CXCR4, a gene previously associated with sprouting endothelial cells. Pharmacological inhibition of CXCR4 signaling suppressed endothelial sprouting and...
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Assert is a website where the best academic papers on arXiv (computer science, math, physics), bioRxiv (biology), BITSS (reproducibility), EarthArXiv (earth science), engrXiv (engineering), LawArXiv (law), PsyArXiv (psychology), SocArXiv (social science), and SportRxiv (sport research) bubble to the top each day.

Papers are scored (in real-time) based on how verifiable they are (as determined by their Github repos) and how interesting they are (based on Twitter).

To see top papers, follow us on twitter @assertpub_ (arXiv), @assert_pub (bioRxiv), and @assertpub_dev (everything else).

To see beautiful figures extracted from papers, follow us on Instagram.

Tracking 225,405 papers.

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Tracking 225,405 papers.