In Candida albicans hyphae, Sec2p is physically associated with SEC2 mRNA on secretory vesicles.

Abstract:

:Candida albicans 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 SEC2 mRNA is physically associated with Sec2p. Moreover, we show that the phosphorylation of S584 allows SEC2 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 SEC2 mRNA on secretory vesicles to the tip localizes SEC2 translation to tip allowing a sufficient accumulation of this key protein at the site of polarized growth.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Caballero-Lima D,Hautbergue GM,Wilson SA,Sudbery PE

doi

10.1111/mmi.12799

subject

Has Abstract

pub_date

2014-11-01 00:00:00

pages

828-42

issue

4

eissn

0950-382X

issn

1365-2958

journal_volume

94

pub_type

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