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A tetrameric complex of membrane proteins in the endoplasmic reticulum.

Authors: Hartmann, E  Gorlich, D  Kostka, S  Otto, A  Kraft, R  Knespel, S  Burger, E  Rapoport, TA  Prehn, S 
Citation: Hartmann E, etal., Eur J Biochem 1993 Jun 1;214(2):375-81.
Pubmed: (View Article at PubMed) PMID:7916687

The translocation site (translocon), at which nascent polypeptides pass through the endoplasmic reticulum membrane, contains a component previously called 'signal sequence receptor' that is now renamed as 'translocon-associated protein' (TRAP). Two glycosylated subunits of the TRAP complex have been identified before (alpha and beta subunits). We now show that TRAP complex is actually comprised of four membrane proteins (alpha, beta, gamma, delta), present in a stoichiometric relation, which are genuine neighbours in intact microsomes. The amino acid sequences of the additional, non-glycosylated subunits were deduced from cloning of the corresponding cDNAs. The delta subunit spans the membrane only once and has its major portion, containing a disulfide bridge, at the lumenal side. The gamma subunit is predicted to span the membrane four times.

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CRRD Object Information
CRRD ID: 61758
Created: 2001-04-10
Species: All species
Last Modified: 2001-04-10
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.