Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8469967 | European Journal of Cell Biology | 2014 | 11 Pages |
Abstract
To address the precise cellular function of JMY in cellular actin rearrangements, we have searched for potential new interaction partners by mass spectrometry. We identified several candidates and correlated their localization with the subcellular dynamics of JMY. JMY is localized to dynamic vesiculo-tubular structures throughout the cytoplasm, which are decorated with actin and Arp2/3 complex. Moreover, JMY partially colocalizes and interacts with VAP-A, which is involved in vesicle-based transport processes. Finally, overexpression of JMY results in Golgi dispersal by loss from the trans-site and affects VSV-G transport. These analyses, together with biochemical experiments, indicate that JMY drives vesicular trafficking in the trans-Golgi region and at ER-membrane contact sites (MCS), distinct from other Arp2/3 activators involved in vesicle transport processes such as the related WHAMM or WASH.
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Authors
Kai Schlüter, Dieter Waschbüsch, Moritz Anft, Debbie Hügging, Sabine Kind, Jan Hänisch, Goran Lakisic, Alexis Gautreau, Angelika Barnekow, Theresia E.B. Stradal,