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In C andida albicans hyphae, S ec2p is physically associated with SEC2 mRNA on secretory vesicles
Author(s) -
CaballeroLima David,
Hautbergue Guillaume M.,
Wilson Stuart A.,
Sudbery Peter E.
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12799
Subject(s) - biology , vesicle , secretory vesicle , microbiology and biotechnology , secretory pathway , golgi apparatus , rab , messenger rna , candida albicans , secretory protein , gtpase , biochemistry , secretion , gene , endoplasmic reticulum , membrane
Summary C andida 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 S ec2p, the G uanine E xchange F actor ( GEF ) for the Rab GTP ase S ec4p. GTP bound S ec4p is required for the transit of secretory vesicles from the trans‐ G olgi to sites of polarized growth. We previously showed that phosphorylation of S ec2p at residue S 584 was necessary for S ec2p to support hyphal, but not yeast growth. Here we show that on secretory vesicles SEC2 mRNA is physically associated with S ec2p. Moreover, we show that the phosphorylation of S 584 allows SEC2 mRNA to dissociate from S ec2p and we speculate that this is necessary for S ec2p 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.