I-BAR (inverse-Bin/amphiphysin/Rvs)-domain-containing proteins such as IRSp53 (insulin receptor substrate of 53 kDa) associate with outwardly curved membranes and connect them to proteins involved in actin dynamics. Research on I-BAR proteins has focussed on possible roles in filopod and lamellipod formation, but their full physiological function remains unclear. The social amoeba Dictyostelium encodes a single I-BAR/SH3 (where SH3 is Src homology 3) protein, called IBARa, along with homologues of proteins that interact with IRSp53 family proteins in mammalian cells, providing an excellent model to study its cellular function. Disruption of the gene encoding IBARa leads to a mild defect in development, but filopod and pseudopod dynamics are unaffected. Furthermore, ectopically expressed IBARa does not induce filopod formation and does not localize to filopods. Instead, IBARa associates with clathrin puncta immediately before they are endocytosed. This role is conserved: human BAIAP2L2 (brain-specific angiogenesis inhibitor 1-associated protein 2-like 2) also tightly co-localizes with clathrin plaques, although its homologues IRSp53 and IRTKS (insulin receptor tyrosine kinase substrate) associate with other punctate structures. The results from the present study suggest that I-BAR-containing proteins help generate the mem-brane curvature required for endocytosis and implies an unexpected role for IRSp53 family proteins in vesicle trafficking.
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Research Article|
April 27 2011
Functional analysis of Dictyostelium IBARa reveals a conserved role of the I-BAR domain in endocytosis
Douwe M. Veltman;
Douwe M. Veltman
*Beatson Institute for Cancer Research, Switchback Road, Bearsden, Glasgow G61 1BD, U.K.
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Giulio Auciello;
Giulio Auciello
†School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Heather J. Spence;
Heather J. Spence
*Beatson Institute for Cancer Research, Switchback Road, Bearsden, Glasgow G61 1BD, U.K.
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Laura M. Machesky;
Laura M. Machesky
*Beatson Institute for Cancer Research, Switchback Road, Bearsden, Glasgow G61 1BD, U.K.
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Joshua Z. Rappoport;
Joshua Z. Rappoport
†School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Robert H. Insall
Robert H. Insall
1
*Beatson Institute for Cancer Research, Switchback Road, Bearsden, Glasgow G61 1BD, U.K.
1To whom correspondence should be addressed (email r.insall@beatson.gla.ac.uk).
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Publisher: Portland Press Ltd
Received:
October 14 2010
Revision Received:
February 28 2011
Accepted:
March 14 2011
Accepted Manuscript online:
March 14 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem J (2011) 436 (1): 45–52.
Article history
Received:
October 14 2010
Revision Received:
February 28 2011
Accepted:
March 14 2011
Accepted Manuscript online:
March 14 2011
Citation
Douwe M. Veltman, Giulio Auciello, Heather J. Spence, Laura M. Machesky, Joshua Z. Rappoport, Robert H. Insall; Functional analysis of Dictyostelium IBARa reveals a conserved role of the I-BAR domain in endocytosis. Biochem J 15 May 2011; 436 (1): 45–52. doi: https://doi.org/10.1042/BJ20101684
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