ArticleCellular and molecular life sciences : CMLS2011
The FN3 and BRCT motifs in the exomer component Chs5p define a conserved module that is necessary and sufficient for its function.
Article in Cellular and molecular life sciences : CMLS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Pck2 association with the plasma membrane and efficient response of the cell integrity pathway require regulation of PI4P homeostasis by exomer.Open biology · 2024Article
- Exomer Is Part of a Hub Where Polarized Secretion and Ionic Stress Connect.Frontiers in microbiology · 2021Article
- Evolutionary cell biology traces the rise of the exomer complex in Fungi from an ancient eukaryotic component.Scientific reports · 2018Article
- Article
- The exomer cargo adaptor structure reveals a novel GTPase-binding domain.The EMBO journal · 2012Article
- Saccharomyces cerevisiae Dbf4 has unique fold necessary for interaction with Rad53 kinase.The Journal of biological chemistry · 2012Article
- BRCT domains: easy as one, two, three.Cell cycle (Georgetown, Tex.) · 2011Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chs5p is a component of the exomer, a coat complex required to transport the chitin synthase Chs3p from the trans-Golgi network to the plasma membrane. The Chs5p N-terminal region exhibits fibronectin type III (FN3) and BRCT domains. FN3 domains are present in proteins that mediate adhesion processes, whereas BRCT domains are involved in DNA repair. Several fungi--including Schizosaccharomyces pombe, which has no detectable amounts of chitin--have proteins similar to Chs5p. Here we show that the FN3 and BRCT motifs in Chs5p behave as a module that is necessary and sufficient for Chs5p localization and for cargo delivery. The N-terminal regions of S. cerevisiae Chs5p and S. pombe Cfr1p are interchangeable in terms of Golgi localization, but not in terms of exomer assembly, showing that the conserved function of this module is protein retention in this organelle and that the interaction between the exomer components is organism-specific.
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