期刊
NATURE CELL BIOLOGY
卷 20, 期 11, 页码 1290-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41556-018-0220-2
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资金
- EU-FP7-Systems Microscopy Network of Excellence [HEALTH-F4-2010-258068]
- EU-H2020-Multimot (EU) [634107]
- Strategic Research Foundation of Sweden [SB16-0046]
- Swedish Research Council [521-2012-3180]
- Swedish Cancer Society
- Cancer Research UK [13329/A21671]
- Knut and Alice Wallenberg Foundation
- BBSRC
- Wellcome Trust
- University of Manchester Strategic Fund
- Centre for Innovative Medicine
- Swedish Foundation for Strategic Research (SSF) [SB16-0046] Funding Source: Swedish Foundation for Strategic Research (SSF)
Adhesion to the extracellular matrix persists during mitosis in most cell types. However, while classical adhesion complexes, such as focal adhesions, do and must disassemble to enable mitotic rounding, the mechanisms of residual mitotic cell-extracellular matrix adhesion remain undefined. Here, we identify 'reticular adhesions', a class of adhesion complex that is mediated by integrin alpha v beta 5, formed during interphase, and preserved at cell-extracellular matrix attachment sites throughout cell division. Consistent with this role, integrin beta 5 depletion perturbs mitosis and disrupts spatial memory transmission between cell generations. Reticular adhesions are morphologically and dynamically distinct from classical focal adhesions. Mass spectrometry defines their unique composition, enriched in phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P-2)-binding proteins but lacking virtually all consensus adhesome components. Indeed, reticular adhesions are promoted by PtdIns(4,5)P-2, and form independently of talin and F-actin. The distinct characteristics of reticular adhesions provide a solution to the problem of maintaining cell-extracellular matrix attachment during mitotic rounding and division.
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