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. 1997 Jun 30;137(7):1483–1493. doi: 10.1083/jcb.137.7.1483

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A model for the interaction between Sec63p and BiP in posttranslational translocation across the ER membrane. (1) Our experiments suggest that BiP is recruited to the translocation apparatus by the lumenal domain of Sec63p. (2) The lumenal domain of Sec63p stimulates ATP hydrolysis by BiP to promote stable binding of BiP to the translocon. BiP may continue to associate with Sec63p while binding to the unfolded precursor protein emerging from the Sec61p pore. (3) The precursor or an unidentified protein then would catalyze nucleotide exchange in the ATP binding site of BiP, allowing BiP to undergo another cycle of interaction with Sec63p. This model does not include other precursor interactions with ER chaperones that may execute final secretory protein folding.