Journal
JOURNAL OF CELL SCIENCE
Volume 127, Issue 17, Pages 3862-3876Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.155663
Keywords
Integrin; Invasion; Lamellipodia; Migration
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Funding
- Associazione Italiana per la Ricerca sul Cancro (AIRC) [IG 10321]
- Telethon Foundation Italy [GGP12126]
- Italian Ministry for Research [20108MXN2J]
- Fondazione Italiana per la Ricerca sul Cancro (FIRC)
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Cell migration during development and metastatic invasion requires the coordination of actin and adhesion dynamics to promote protrusive activity at the front of the cell. The knowledge of the molecular mechanisms required to achieve such coordination is fragmentary. Here, we identify a new functional complex that drives cell motility. ERC1a (an isoform of ERC1) and the LL5 proteins LL5 alpha and LL5 beta (encoded by PHLDB1 and PHLDB2, respectively) are required, together with liprin-alpha 1, for effective migration and tumor cell invasion, and do so by stabilizing the protrusive activity at the cell front. Depletion of either protein negatively affects invasion, migration on extracellular matrix, lamellipodial persistence and the internalization of active integrin beta 1 receptors needed for adhesion turnover at the front of the cell. Liprin-alpha 1, ERC1a and LL5 also define new highly polarized and dynamic cytoplasmic structures uniquely localized near the protruding cell edge. Our results indicate that the functional complex and the associated structures described here represent an important mechanism to drive tumor cell migration.
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