Urbanek, A.N., Chan, R. and Ayscough, K.R. (2015) Function and interactions of the Ysc84/SH3yl1 family of actin- and lipid-binding proteins. Biochemical Society Transactions, 43. 111 - 116. ISSN 0300-5127
Abstract
Understanding how actin filaments are nucleated, polymerized and disassembled in close proximity to cell membranes is an area of growing interest. Protrusion of the plasma membrane is required for cell motility, whereas inward curvature or invagination is required for endocytic events. These morphological changes in membrane are often associated with rearrangements of actin, but how the many actin-binding proteins of eukaryotes function in a co-ordinated way to generate the required responses is still not well understood. Identification and analysis of proteins that function at the interface between the plasma membrane and actin-regulatory networks is central to increasing our knowledge of the mechanisms required to transduce the force of actin polymerization to changes in membrane morphology. The Ysc84/SH3yl1 proteins have not been extensively studied, but work in both yeast and mammalian cells indicate that these proteins function at the hub of networks integrating regulation of filamentous actin (F-actin) with changes in membrane morphology.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © The Authors Journal compilation © 2015 Biochemical Society. This is an author produced version of a paper subsequently published in Biochemical Society Transactions. Uploaded in accordance with the publisher's self-archiving policy. |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Biomedical Science (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 27 May 2015 12:47 |
Last Modified: | 04 Nov 2017 02:30 |
Published Version: | http://dx.doi.org/10.1042/BST20140221 |
Status: | Published |
Publisher: | Portland Press |
Refereed: | Yes |
Identification Number: | 10.1042/BST20140221 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:85426 |