[SRPRB_MOUSE] Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. Has GTPase activity. May mediate the membrane association of SRPR. [SRP54_CANFA] Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein). [SRPR_HUMAN] Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system.
Evolutionary Conservation
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Publication Abstract from PubMed
Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by docking with the SRP receptor, which facilitates transfer of the ribosome to the translocon. Here, we present the 8 angstrom cryo-electron microscopy structure of a "docking complex" consisting of a SRP-bound 80S ribosome and the SRP receptor. Interaction of the SRP receptor with both SRP and the ribosome rearranged the S domain of SRP such that a ribosomal binding site for the translocon, the L23e/L35 site, became exposed, whereas Alu domain-mediated elongation arrest persisted.
Signal recognition particle receptor exposes the ribosomal translocon binding site.,Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R Science. 2006 May 5;312(5774):745-7. PMID:16675701[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R. Signal recognition particle receptor exposes the ribosomal translocon binding site. Science. 2006 May 5;312(5774):745-7. PMID:16675701 doi:312/5774/745
