ArticleMolecular microbiology2014
In Candida albicans hyphae, Sec2p is physically associated with SEC2 mRNA on secretory vesicles.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Post-transcriptional control of fungal cell wall synthesis.Cell surface (Amsterdam, Netherlands) · 2022Article
- Hitchhiking Across Kingdoms: Cotransport of Cargos in Fungal, Animal, and Plant Cells.Annual review of cell and developmental biology · 2022Review
- From Jekyll to Hyde: The Yeast-Hyphal Transition ofPathogens (Basel, Switzerland) · 2021Review
- The 5' Untranslated Region of themSphere · 2018Article
- Messenger RNA transport in the opportunistic fungal pathogen Candida albicans.Current genetics · 2017Review
- Post-translational modification directs nuclear and hyphal tip localization of Candida albicans mRNA-binding protein Slr1.Molecular microbiology · 2017Article
- Hitchhiking: A Non-Canonical Mode of Microtubule-Based Transport.Trends in cell biology · 2017Review
- Control of Candida albicans morphology and pathogenicity by post-transcriptional mechanisms.Cellular and molecular life sciences : CMLS · 2016Review
- Genome-Wide Transcription Study of Cryptococcus neoformans H99 Clinical Strain versus Environmental Strains.PloS one · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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.
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