Member database | CDD |
CDD type | domain |
Short name | Myo5_CBD |
Set | Myo5-like_CBD |
Description
Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.
[4, 5, 2, 1, 3]References
1.She3p binds to the rod of yeast myosin V and prevents it from dimerizing, forming a single-headed motor complex. Hodges AR, Krementsova EB, Trybus KM. J Biol Chem 283, 6906-14, (2008). PMID: 18175803
2.Functions of class V myosins in neurons. Hammer JA 3rd, Wagner W. J. Biol. Chem. 288, 28428-34, (2013). View articlePMID: 23990471
3.Myosin V from head to tail. Trybus KM. Cell. Mol. Life Sci. 65, 1378-89, (2008). View articlePMID: 18239852
4.Structure of a myosin•adaptor complex and pairing by cargo. Shi H, Singh N, Esselborn F, Blobel G. Proc. Natl. Acad. Sci. U.S.A. 111, E1082-90, (2014). View articlePMID: 24522109