ArticleThe EMBO journal1998
Distinct functions of calmodulin are required for the uptake step of receptor-mediated endocytosis in yeast: the type I myosin Myo5p is one of the calmodulin targets.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 60 citations in OpenAlex.
- Endocytic myosin-1 is a force-insensitive, power-generating motor.The Journal of cell biology · 2023Article
- Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023Article
- Yeast-model-based study identified myosin- and calcium-dependent calmodulin signalling as a potential target for drug intervention in chorea-acanthocytosis.Disease models & mechanisms · 2019Article
- Calmodulin Promotes N-BAR Domain-Mediated Membrane Constriction and Endocytosis.Developmental cell · 2016Article
- Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites.The EMBO journal · 2010Article
- Finding friends and enemies in an enemies-only network: a graph diffusion kernel for predicting novel genetic interactions and co-complex membership from yeast genetic interactions.Genome research · 2008Article
- Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Synthesis and function of membrane phosphoinositides in budding yeast, Saccharomyces cerevisiae.Biochimica et biophysica acta · 2007Review
- Developmental change in the calcium sensor for synaptic vesicle endocytosis in central nerve terminals.Journal of neurochemistry · 2005Article
- Functional characterization of myosin I tail regions in Candida albicans.Eukaryotic cell · 2004Article
- Binding of calmodulin to Nuf1p is required for karyogamy in Saccharomyces cerevisiae.Molecular genetics and genomics : MGG · 2003Article
- Cofilin, but not profilin, is required for myosin-I-induced actin polymerization and the endocytic uptake in yeast.Molecular biology of the cell · 2002Article
- Calmodulin controls organization of the actin cytoskeleton via regulation of phosphatidylinositol (4,5)-bisphosphate synthesis in Saccharomyces cerevisiae.The Biochemical journal · 2002Article
- Remodeling of organelle-bound actin is required for yeast vacuole fusion.The Journal of cell biology · 2002Article
- Multiple functions of sterols in yeast endocytosis.Molecular biology of the cell · 2002Article
- An intact SH3 domain is required for myosin I-induced actin polymerization.The EMBO journal · 2000Article
- Increased protein kinase or decreased PP2A activity bypasses sphingoid base requirement in endocytosis.The EMBO journal · 2000Article
- Functional interactions between the p35 subunit of the Arp2/3 complex and calmodulin in yeast.Molecular biology of the cell · 2000Article
- A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex.The Journal of cell biology · 2000Article
- Polarized sphingolipid transport from the subapical compartment: evidence for distinct sphingolipid domains.Molecular biology of the cell · 1999Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The uptake step of receptor-mediated endocytosis in yeast is dependent on the calcium binding protein calmodulin (Cmd1p). In order to understand the role that Cmd1p plays, a search was carried out for possible targets among the genes required for the internalization process. Co-immunoprecipitation, two-hybrid and overlay assays demonstrated that Cmd1p interacts with Myo5p, a type I unconventional myosin. Analysis of the endocytic phenotype and the Cmd1p-Myo5p interaction in thermosensitive cmd1 mutants indicated that the Cmd1p-Myo5p interaction is required for endocytosis in vivo. However, the Cmd1p-Myo5p interaction requirement was partially overcome by deleting the calmodulin binding sites (IQ motifs) from Myo5p, suggesting that these motifs inhibit Myo5p function. Additionally, genetic and biochemical evidence obtained with a collection of cmd1 mutant alleles strongly suggests that Cmd1p plays an additional role in the internalization step of receptor-mediated endocytosis in yeast.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.