In Candida albicans hyphae, Sec2p is physically associated with SEC2 mRNA on secretory vesicles. Issue 4 (14th October 2014)

• Record Type: Journal Article
• Authors: Caballero‐Lima, David; Hautbergue, Guillaume M.; Wilson, Stuart A.; Sudbery, Peter E.
• Is Part Of: Molecular microbiology. Volume 94:Issue 4(2014)
• Page Start: 828
• Page End: 842
• Publication Date: 2014-10-14
• Subjects: Molecular microbiology -- Periodicals; 572.829
• DOI: 10.1111/mmi.12799
• Languages: English
• ISSNs: 0950-382X

Abstract

<abstract abstract-type="main"> <title>Summary</title> <p> <italic>C</italic> <italic>andida albicans</italic> hyphae grow in a highly polarized fashion from their tips. This polarized growth requires the continuous delivery of secretory vesicles to the tip region. Vesicle delivery depends on Sec2p, the Guanine Exchange Factor (GEF) for the Rab GTPase Sec4p. GTP bound Sec4p is required for the transit of secretory vesicles from the trans‐Golgi to sites of polarized growth. We previously showed that phosphorylation of Sec2p at residue S584 was necessary for Sec2p to support hyphal, but not yeast growth. Here we show that on secretory vesicles <italic>SEC2</italic> mRNA is physically associated with Sec2p. Moreover, we show that the phosphorylation of S584 allows <italic>SEC2</italic> mRNA to dissociate from Sec2p and we speculate that this is necessary for Sec2p function and/or translation. During hyphal extension, the growing tip may be separated from the nucleus by up to 15 μm. Transport of <italic>SEC2</italic> mRNA on secretory vesicles to the tip localizes <italic>SEC2</italic> translation to tip allowing a sufficient accumulation of this key protein at the site of polarized growth.</p> </abstract>