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PMID:20647997

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Citation

Grötsch, H, Giblin, JP, Idrissi, FZ, Fernández-Golbano, IM, Collette, JR, Newpher, TM, Robles, V, Lemmon, SK and Geli, MI (2010) Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites. EMBO J. 29:2899-914

Abstract

Myosins-I are conserved proteins that bear an N-terminal motor head followed by a Tail Homology 1 (TH1) lipid-binding domain. Some myosins-I have an additional C-terminal extension (C(ext)) that promotes Arp2/3 complex-dependent actin polymerization. The head and the tail are separated by a neck that binds calmodulin or calmodulin-related light chains. Myosins-I are known to participate in actin-dependent membrane remodelling. However, the molecular mechanisms controlling their recruitment and their biochemical activities in vivo are far from being understood. In this study, we provided evidence suggesting the existence of an inhibitory interaction between the TH1 domain of the yeast myosin-I Myo5 and its C(ext). The TH1 domain prevented binding of the Myo5 C(ext) to the yeast WIP homologue Vrp1, Myo5 C(ext)-induced actin polymerization and recruitment of the Myo5 C(ext) to endocytic sites. Our data also indicated that calmodulin dissociation from Myo5 weakened the interaction between the neck and TH1 domains and the C(ext). Concomitantly, calmodulin dissociation triggered Myo5 binding to Vrp1, extended the myosin-I lifespan at endocytic sites and activated Myo5-induced actin polymerization.

Links

PubMed PMC2944048 Online version:10.1038/emboj.2010.159

Keywords

Actin-Related Protein 2-3 Complex/metabolism; Calmodulin/metabolism; Endocytosis; Microfilament Proteins/metabolism; Myosin Type I/metabolism; Protein Binding; Protein Interaction Domains and Motifs; Protein Multimerization; Saccharomyces cerevisiae/physiology; Saccharomyces cerevisiae Proteins/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

YEAST:CALM

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q04439

F

Seeded From UniProt

complete

YEAST:VRP1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q04439

F

Seeded From UniProt

complete

YEAST:RV167

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q04439

F

Seeded From UniProt

complete

YEAST:MYO5

located_in

GO:0030479: actin cortical patch

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

YEAST:MYO5

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P06787

F

Seeded From UniProt

complete

YEAST:MYO5

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P37370

F

Seeded From UniProt

complete

YEAST:MYO5

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P39743

F

Seeded From UniProt

complete

YEAST:MYO5

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q04439

F

Seeded From UniProt

complete

YEAST:MYO5

part_of

GO:0030479: actin cortical patch

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete


See also

References

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