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Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells




TekijätBertling E, Hotulainen P, Mattila PK, Matilainen T, Salminen M, Lappalainen P

KustantajaAMER SOC CELL BIOLOGY

Julkaisuvuosi2004

JournalMolecular Biology of the Cell

Tietokannassa oleva lehden nimiMOLECULAR BIOLOGY OF THE CELL

Lehden akronyymiMOL BIOL CELL

Vuosikerta15

Numero5

Aloitussivu2324

Lopetussivu2334

Sivujen määrä11

ISSN1059-1524

DOIhttps://doi.org/10.1091/mbc.E04-01-0048


Tiivistelmä
Cyclase-associated proteins (CAPs) are highly conserved actin monomer binding proteins present in all eukaryotes. However, the mechanism by which CAPs contribute to actin dynamics has been elusive. In mammals, the situation is further complicated by the presence of two CAP isoforms whose differences have not been characterized. Here, we show that CAP1 is widely expressed in mouse nonmuscle cells, whereas CAP2 is the predominant isoform in developing striated muscles. In cultured NIH3T3 and 1316171 cells, CAP1 is a highly abundant protein that colocalizes with cofilin-1 to dynamic regions of the cortical actin cytoskeleton. Analysis of CAP1 knockdown cells demonstrated that this protein promotes rapid actin filament depolymerization and is important for cell morphology, migration, and endocytosis. Interestingly, depletion of CAP1 leads to an accumulation of cofilin-1 into abnormal cytoplasmic aggregates and to similar cytoskeletal defects to those seen in cofilin-1 knockdown cells, demonstrating that CAP1 is required for proper subcellular localization and function of ADF/cofilin. Together, these data provide the first direct in vivo evidence that CAP promotes rapid actin dynamics in conjunction with ADF/cofilin and is required for several central cellular processes in mammals.

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