Palmer, S.E. and Smaczynska-de Rooij, I.I. and Marklew, C.J. and Allwood, E.G. and Mishra, R. and Goldberg, M.W. and Ayscough, K.R. (2015) 'A Charge Swap mutation E461K in the yeast dynamin Vps1 reduces endocytic invagination.', Communicative & integrative biology., 8 (4). e1051274.
Vps1 is the yeast dynamin-like protein that functions during several membrane trafficking events including traffic from Golgi to vacuole, endosomal recycling and endocytosis. Vps1 can also function in peroxisomal fission indicating that its ability to drive membrane fission is relatively promiscuous. It has been of interest therefore that several mutations have been identified in Vps1 that only disrupt its endocytic function. Most recently, disruption of the interaction with actin through mutation of residues in one of the central stalk α helices (RR457,458 EE) has been shown to disrupt endocytosis and cause an accumulation of highly elongated invaginations in cells. This data supports the idea that an interaction between Vps1 and actin is important to drive the scission stage in endocytosis. Another Vps1 mutant generated in the study was vps1 E461K. Here we show data demonstrating that the E461K mutation also disrupts endocytosis but at an early stage, resulting in inhibition of the invagination step itself.
|Keywords:||Dynamin, Dynamin-like protein, Endocytosis, Membrane trafficking.|
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|Publisher Web site:||http://dx.doi.org/10.1080/19420889.2015.1051274|
|Publisher statement:||© Sarah E Palmer, Iwona I Smaczynska-de Rooij, Christopher J Marklew, Ellen G Allwood, Ritu Mishra, Martin W Goldberg, and Kathryn R Ayscough This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.|
|Record Created:||20 Nov 2015 15:35|
|Last Modified:||20 Nov 2015 15:39|
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