ArticleMolecular biology of the cell2011
Dysregulated Arl1, a regulator of post-Golgi vesicle tethering, can inhibit endosomal transport and cell proliferation in yeast.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- The SNARE-associated protein Sft2 functions in Imh1-mediated SNARE recycling transport upon ER stress.Molecular biology of the cell · 2023Article
- Insights into the Conserved Regulatory Mechanisms of Human and Yeast Aging.Biomolecules · 2020Review
- Overexpression ofSmall GTPases · 2020Article
- Action of Arl1 GTPase and golgin Imh1 in Ypt6-independent retrograde transport from endosomes to the trans-Golgi network.Molecular biology of the cell · 2019Article
- Role of Arf GTPases in fungal morphogenesis and virulence.PLoS pathogens · 2017Article
- The TRAPP Subunit Trs130p Interacts with the GAP Gyp6p to Mediate Ypt6p Dynamics at the Late Golgi.Frontiers in cell and developmental biology · 2016Article
- Article
- The Arf family G protein Arl1 is required for secretory granule biogenesis in Drosophila.Journal of cell science · 2014Article
- Env7p Associates with the Golgin Protein Imh1 at the trans-Golgi Network in Candida albicans.mSphereArticle
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
Small monomeric G proteins regulated in part by GTPase-activating proteins (GAPs) are molecular switches for several aspects of vesicular transport. The yeast Gcs1 protein is a dual-specificity GAP for ADP-ribosylation factor (Arf) and Arf-like (Arl)1 G proteins, and also has GAP-independent activities. The absence of Gcs1 imposes cold sensitivity for growth and endosomal transport; here we present evidence that dysregulated Arl1 may cause these impairments. We show that gene deletions affecting the Arl1 or Ypt6 vesicle-tethering pathways prevent Arl1 activation and membrane localization, and restore growth and trafficking in the absence of Gcs1. A mutant version of Gcs1 deficient for both ArfGAP and Arl1GAP activity in vitro still allows growth and endosomal transport, suggesting that the function of Gcs1 that is required for these processes is independent of GAP activity. We propose that, in the absence of this GAP-independent regulation by Gcs1, the resulting dysregulated Arl1 prevents growth and impairs endosomal transport at low temperatures. In cells with dysregulated Arl1, an increased abundance of the Arl1 effector Imh1 restores growth and trafficking, and does so through Arl1 binding. Protein sequestration at the trans-Golgi membrane by dysregulated, active Arl1 may therefore be the mechanism of inhibition.
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