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Members of the CIP4 family of proteins participate in the regulation of platelet-derived growth factor receptor-beta-dependent actin reorganization and migration
Department of Microbiology, Tumor and Cell Biology Karolinska Institute, Box 280 SE-171 77 Stockholm.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm , Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm , Ludwig Institute for Cancer Research.
Department of Microbiology, Tumor and Cell Biology Karolinska Institute, Box 280 SE-171 77 Stockholm.
2010 (English)In: Biology of the Cell, ISSN 0248-4900, E-ISSN 1768-322X, Vol. 102, no 4, 215-230 p.Article in journal (Refereed) Published
Abstract [en]

BACKGROUND INFORMATION: The F-BAR {Fes/CIP4 [Cdc42 (cell division cycle 42)-interacting protein 4] homology and BAR (Bin/amphiphysin/Rvs)} proteins have emerged as important co-ordinators of signalling pathways that regulate actin assembly and membrane dynamics. The presence of the F-BAR domain is the hallmark of this family of proteins and the CIP4 (Cdc42-interacting protein 4) was one of the first identified vertebrate F-BAR proteins. There are three human CIP4 paralogues, namely CIP4, FBP17 (formin-binding protein 17) and Toca-1 (transducer of Cdc42-dependent actin assembly 1). The CIP4-like proteins have been implicated in Cdc42-dependent actin reorganization and in regulation of membrane deformation events visible as tubulation of lipid bilayers. RESULTS: We performed side-by-side analyses of the three CIP4 paralogues. We found that the three CIP4-like proteins vary in their effectiveness to catalyse membrane tubulation and actin reorganization. Moreover, we show that the CIP4-dependent membrane tubulation is enhanced in the presence of activated Cdc42. Some F-BAR members have been shown to have a role in the endocytosis of the EGF (epidermal growth factor) receptor and this prompted us to study the involvement of the CIP4-like proteins in signalling of the PDGFRbeta [PDGF (platelet-derived growth factor) beta-receptor]. We found that knock-down of CIP4-like proteins resulted in a prolonged formation of PDGF-induced dorsal ruffles, as well as an increased PDGF-dependent cell migration. This was most likely a consequence of a sustained PDGFRbeta activation caused by delayed internalization of the receptor in the cells treated with siRNA (small interfering RNA) specific for the CIP4-like proteins. CONCLUSIONS: Our findings show that CIP4-like proteins induced membrane tubulation downstream of Cdc42 and that they have important roles in PDGF-dependent actin reorganization and cell migration by regulating internalization and activity of the PDGFRbeta. Moreover, the results suggest an important role for the CIP4-like proteins in the regulation of the activity of the PDGFRbeta.

Place, publisher, year, edition, pages
Portland Press Limited , 2010. Vol. 102, no 4, 215-230 p.
Keyword [en]
actin, cell division cycle 42 (Cdc42), Cdc42-interacting protein 4 (CIP4), formin-binding protein 17 (FBP17), membrane tubulation, Rho, transducer of Cdc42-dependent actin assembly 1 (Toca-1)
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-131263DOI: 10.1042/BC20090033ISI: 000276733400002PubMedID: 19909236OAI: oai:DiVA.org:uu-131263DiVA: diva2:353848
Available from: 2010-09-29 Created: 2010-09-29 Last updated: 2017-12-12Bibliographically approved

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