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Pombe Cdc15 homology proteins: regulators of membrane dynamics and the actin cytoskeleton
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.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm , Ludwig Institute for Cancer Research.
2006 (English)In: TIBS -Trends in Biochemical Sciences. Regular ed., ISSN 0968-0004, E-ISSN 1362-4326, Vol. 31, no 12, 670-679 p.Article, review/survey (Refereed) Published
Abstract [en]

Pombe Cdc15 homology (PCH) proteins have emerged in many species as important coordinators of signalling pathways that regulate actomyosin assembly and membrane dynamics. For example, the prototype PCH protein, Cdc15p of Schizosaccharomyces pombe, has a role in assembly of the contractile ring, which is needed to separate dividing cells. Recently, mammalian PCH proteins have been found to bind phospholipids and to participate in membrane deformation. These findings suggest that PCH proteins are crucial linkers of membrane dynamics and actin polymerization, for example, during the internalization of transmembrane receptors. Intriguingly, some members of the PCH protein family are mutated in neurodegenerative and inflammatory diseases, which has implications for the identification of cures for such disorders.

Place, publisher, year, edition, pages
2006. Vol. 31, no 12, 670-679 p.
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Medical and Health Sciences
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URN: urn:nbn:se:uu:diva-19719DOI: 10.1016/j.tibs.2006.10.001ISI: 000242873100004PubMedID: 17074490OAI: oai:DiVA.org:uu-19719DiVA: diva2:47491
Available from: 2006-12-01 Created: 2006-12-01 Last updated: 2017-12-08Bibliographically approved

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Aspenström, PontusFransson, ÅsaRichnau, Ninna

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