uu.seUppsala University Publications
Change search
ReferencesLink to record
Permanent link

Direct link
Roles of F-BAR/PCH Proteins in the Regulation of Membrane Dynamics and Actin Reorganization
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm , Ludwig Institute for Cancer Research.
2009 (English)In: International Review of Cell and Molecular Biology, Vol. 272, 1-31 p.Article, review/survey (Refereed) Published
Abstract [en]

The Pombe Cdc15 Homology (PCH) proteins have emerged in many species as important coordinators of signaling pathways that regulate actomyosin assembly and membrane dynamics. The hallmark of the PCH proteins is the presence of a Fes/ClP4 homology-Bin/Amphiphysin/Rvsp (F-BAR) domain; therefore they are commonly referred to as F-BAR proteins. The prototype F-BAR protein, Cdc15p of Schizosaccharomyces pombe, has a role in the formation of the contractile actomyosin ring during cytokinesis. Vertebrate F-BAR proteins have an established role in binding phospholipids and they participate in membrane deformations, for instance, during the internalization of transmembrane receptors. This way the F-BAR proteins will function as linkers between the actin polymerization apparatus and the machinery regulating membrane dynamics. Interestingly, some members of the F-BAR proteins are implicated in inflammatory or neurodegenerative disorders and the observations can be expected to have clinical implications for the treatment of the diseases.

Place, publisher, year, edition, pages
2009. Vol. 272, 1-31 p.
Keyword [en]
Pombe Cdc15 Homology proteins, F-BAR proteins, Actomyosin assembly, Membrane dynamics, Cytoskeleton
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-152218DOI: 10.1016/S1937-6448(08)01601-8ISI: 000262432100001PubMedID: 19121815OAI: oai:DiVA.org:uu-152218DiVA: diva2:413011
Available from: 2011-04-27 Created: 2011-04-27 Last updated: 2011-04-27Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed
By organisation
Ludwig Institute for Cancer Research
Medical and Health Sciences

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 108 hits
ReferencesLink to record
Permanent link

Direct link