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Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex. | LitMetric

AI Article Synopsis

  • Tail-anchored (TA) proteins play crucial roles in various cellular functions such as trafficking, degradation, and apoptosis, and they rely on a C-terminal membrane anchor for their delivery.
  • The delivery process involves the Get3 ATPase interacting with the Get1/2 receptor on the endoplasmic reticulum (ER) membrane.
  • Crystal structures of Get3 in complex with Get1 and Get2 reveal how these receptors bind simultaneously and enable structural changes necessary for the insertion of TA proteins, suggesting a nucleotide-regulated delivery mechanism.

Article Abstract

Tail-anchored (TA) proteins are involved in cellular processes including trafficking, degradation, and apoptosis. They contain a C-terminal membrane anchor and are posttranslationally delivered to the endoplasmic reticulum (ER) membrane by the Get3 adenosine triphosphatase interacting with the hetero-oligomeric Get1/2 receptor. We have determined crystal structures of Get3 in complex with the cytosolic domains of Get1 and Get2 in different functional states at 3.0, 3.2, and 4.6 angstrom resolution. The structural data, together with biochemical experiments, show that Get1 and Get2 use adjacent, partially overlapping binding sites and that both can bind simultaneously to Get3. Docking to the Get1/2 complex allows for conformational changes in Get3 that are required for TA protein insertion. These data suggest a molecular mechanism for nucleotide-regulated delivery of TA proteins.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3601824PMC
http://dx.doi.org/10.1126/science.1207125DOI Listing

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