AI Article Synopsis
- - The Arp2/3 complex creates branched actin networks that push against cellular membranes, playing a vital role in endosomal function and receptor transport.
- - The study identifies HSBP1 as a key protein that helps assemble the WASH complex by breaking apart its precursor, which is necessary for cellular processes at the centrosome.
- - Depleting HSBP1 leads to similar effects as depleting WASH, impacting cell adhesion, polarity, and tumor cell behavior, with high levels of HSBP1 in breast tumors linked to worse patient outcomes.
Article Abstract
The Arp2/3 complex generates branched actin networks that exert pushing forces onto different cellular membranes. WASH complexes activate Arp2/3 complexes at the surface of endosomes and thereby fission transport intermediates containing endocytosed receptors, such as α5β1 integrins. How WASH complexes are assembled in the cell is unknown. Here, we identify the small coiled-coil protein HSBP1 as a factor that specifically promotes the assembly of a ternary complex composed of CCDC53, WASH, and FAM21 by dissociating the CCDC53 homotrimeric precursor. HSBP1 operates at the centrosome, which concentrates the building blocks. HSBP1 depletion in human cancer cell lines and in amoebae phenocopies WASH depletion, suggesting a critical role of the ternary WASH complex for WASH functions. HSBP1 is required for the development of focal adhesions and of cell polarity. These defects impair the migration and invasion of tumor cells. Overexpression of HSBP1 in breast tumors is associated with increased levels of WASH complexes and with poor prognosis for patients.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6028030 | PMC |
| http://dx.doi.org/10.15252/embj.201797706 | DOI Listing |
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