Publication details for Dr Martin GoldbergPalmer, S.E., Smaczynska-de Rooij, I.I., Marklew, C.J., Allwood, E.G., Mishra, R., Goldberg, M.W. & Ayscough, K.R. (2015). A Charge Swap mutation E461K in the yeast dynamin Vps1 reduces endocytic invagination. Communicative & Integrative Biology 8(4): e1051274.
- Publication type: Journal Article
- ISSN/ISBN: 1942-0889 (electronic)
- DOI: 10.1080/19420889.2015.1051274
- Keywords: Dynamin, Dynamin-like protein, Endocytosis, Membrane trafficking.
- Further publication details on publisher web site
- Durham Research Online (DRO) - may include full text
Author(s) from Durham
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.