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Gene Review: 

Myrip  -  myosin VIIA and Rab interacting protein

Mus musculus

Synonyms: A230081N12Rik, Exophilin-8, Myosin-VIIa-and Rab-interacting protein, Rab effector MyRIP, SlaC2-c, ...
 
 
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High impact information on Myrip

  • Based on these findings, we propose that Slac2-c acts as a functional myosin VIIa receptor and that the Rab27A.Slac2-c x myosin VIIa tripartite protein complex regulates the transport of retinal melanosomes in pigment epithelium cells [1].
  • In this study, we discovered that Slac2-a and a closely related isoform, Slac2-c/MyRIP, contain multiple PEST-like sequences (potential signals for rapid protein degradation) in the myosin Va- and actin-binding domains at the C terminus [2].
  • In this chapter we describe the methods that have been used to analyze the protein-protein interactions of Slac2-c, specifically with Rab27A, myosin Va/VIIa, and actin [3].
  • Slac2-c/MyRIP is a specific Rab27A-binding protein that contains an N-terminal synaptotagmin-like protein (Slp) homology domain (SHD, a newly identified GTP-Rab27A-binding motif), but in contrast to the Slp family proteins, it lacks C-terminal tandem C2 domains [3].
 

Anatomical context of Myrip

References

  1. Functional analysis of Slac2-c/MyRIP as a linker protein between melanosomes and myosin VIIa. Kuroda, T.S., Fukuda, M. J. Biol. Chem. (2005) [Pubmed]
  2. Slac2-a/melanophilin contains multiple PEST-like sequences that are highly sensitive to proteolysis. Fukuda, M., Itoh, T. J. Biol. Chem. (2004) [Pubmed]
  3. Identification and biochemical analysis of Slac2-c/MyRIP as a Rab27A-, myosin Va/VIIa-, and actin-binding protein. Kuroda, T.S., Fukuda, M. Meth. Enzymol. (2005) [Pubmed]
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