4lx2
From Proteopedia
Crystal structure of Myo5a globular tail domain in complex with melanophilin GTBD
Structural highlights
DiseaseMYO5A_HUMAN Griscelli disease type 3;Neuroectodermal melanolysosomal disease;Griscelli disease type 1. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. FunctionMYO5A_HUMAN Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.[1] Publication Abstract from PubMedSpecific recognition of the cargo that molecular motors transport or tether to cytoskeleton tracks allows them to perform precise cellular functions at particular times and positions in cells. However, very little is known about how evolution has favored conservation of functions for some isoforms, while also allowing for the generation of new recognition sites and specialized cellular functions. Here we present several crystal structures of the myosin Va or the myosin Vb globular tail domain (GTD) that gives insights into how the motor is linked to the recycling membrane compartments via Rab11 or to the melanosome membrane via recognition of the melanophilin adaptor that binds to Rab27a. The structures illustrate how the Rab11-binding site has been conserved during evolution and how divergence at another site of the GTD allows more specific interactions such as the specific recognition of melanophilin by the myosin Va isoform. With atomic structural insights, these structures also show how either the partner or the GTD structural plasticity upon association is critical for selective recruitment of the motor. Structural basis of myosin V Rab GTPase-dependent cargo recognition.,Pylypenko O, Attanda W, Gauquelin C, Lahmani M, Coulibaly D, Baron B, Hoos S, Titus MA, England P, Houdusse AM Proc Natl Acad Sci U S A. 2013 Nov 18. PMID:24248336[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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