ArticleMolecular biology of the cell2006
Regulated phosphorylation of budding yeast's essential myosin V heavy chain, Myo2p.
Article in Molecular biology of the cell, 2006. 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, 18 citations in OpenAlex.
- MYO5A-mediated stabilization promotes the acquisition of fusion competence in sealed autophagosomes.The EMBO journal · 2026Article
- Spatiotemporal regulation of organelle transport by spindle position checkpoint kinase Kin4.Journal of cell science · 2024Article
- Fibrinolytic-deficiencies predispose hosts to septicemia from a catheter-associated UTI.Nature communications · 2024Article
- Post-translational modifications of proteins associated with yeast peroxisome membrane: An essential mode of regulatory mechanism.Genes to cells : devoted to molecular & cellular mechanisms · 2021Review
- Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021Review
- The tail domain of theJournal of cell science · 2018Article
- Novel mechanism coupling cyclic AMP-protein kinase A signaling and golgi trafficking via Gyp1 phosphorylation in polarized growth.Eukaryotic cell · 2014Article
- Overlap of cargo binding sites on myosin V coordinates the inheritance of diverse cargoes.The Journal of cell biology · 2012Article
- PTC1 is required for vacuole inheritance and promotes the association of the myosin-V vacuole-specific receptor complex.Molecular biology of the cell · 2009Article
- The cyclin-dependent kinase Cdk1 directly regulates vacuole inheritance.Developmental cell · 2008Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The tail of the yeast myosin V encoded by Myo2p is known to bind several receptors for cargo delivery along polarized actin cables. However, it is not known how Myo2p activity is regulated or how it selects between cargoes. Here we show that Myo2p is reversibly phosphorylated in vivo. A short peptide at the N-terminal end of the cargo-binding domain contains three residues contributing to single or doubly phosphorylated species. We confirm that the tail consists of two proteolytically resistant subdomains and identify a functionally important region N-terminal to subdomain 1 that includes the phosphorylation sites. Mutagenesis of the phosphorylation sites to alanine abolished a mobility shift diagnostic of phosphorylation, whereas mutagenesis to glutamic acid produced the shift and the formation of an additional phosphorylated species. These substitutions did not affect overall cell growth. However, one of the sites is predicted to be a substrate of cAMP-dependent protein kinase (PKA), and yeast expressing Myo2p with alanine substitutions is resistant to otherwise lethal overexpression of PKA, whereas the glutamic acid mutant is supersensitive to overexpression of PKA. These results suggest that in yeast, Myo2p is subject to phosphoregulation involving a PKA-related signaling pathway.
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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.