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Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum.
Nature. 1994 Aug 04; 370(6488):373-5.Nat

Abstract

During their transit through the endoplasmic reticulum, newly synthesized light and heavy chains of immunoglobulins associate with two endoplasmic reticulum stress proteins. BiP/GRP78, a member of the HSP70 family, binds these polypeptides, presumably through promiscuously exposed hydrophobic sequences, soon after their translocation into the endoplasmic reticulum. GRP94, another endoplasmic reticulum stress protein homologous to HSP90, also associates with unassembled immunoglobulin chains, but its interaction is biochemically, kinetically and structurally distinct from BiP's. We report here that whereas BiP preferentially binds an early disulphide intermediate of light chain and dissociates within a few minutes, GRP94 exclusively binds fully oxidized molecules and dissociates with a half-time of 50 min. These results indicate that GRP94 is itself a chaperone which acts after BiP.

Authors+Show Affiliations

Department of Immunology, Duke University Medical Center, Durham, North Carolina 27710.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7913987

Citation

Melnick, J, et al. "Sequential Interaction of the Chaperones BiP and GRP94 With Immunoglobulin Chains in the Endoplasmic Reticulum." Nature, vol. 370, no. 6488, 1994, pp. 373-5.
Melnick J, Dul JL, Argon Y. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature. 1994;370(6488):373-5.
Melnick, J., Dul, J. L., & Argon, Y. (1994). Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature, 370(6488), 373-5.
Melnick J, Dul JL, Argon Y. Sequential Interaction of the Chaperones BiP and GRP94 With Immunoglobulin Chains in the Endoplasmic Reticulum. Nature. 1994 Aug 4;370(6488):373-5. PubMed PMID: 7913987.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. AU - Melnick,J, AU - Dul,J L, AU - Argon,Y, PY - 1994/8/4/pubmed PY - 1994/8/4/medline PY - 1994/8/4/entrez SP - 373 EP - 5 JF - Nature JO - Nature VL - 370 IS - 6488 N2 - During their transit through the endoplasmic reticulum, newly synthesized light and heavy chains of immunoglobulins associate with two endoplasmic reticulum stress proteins. BiP/GRP78, a member of the HSP70 family, binds these polypeptides, presumably through promiscuously exposed hydrophobic sequences, soon after their translocation into the endoplasmic reticulum. GRP94, another endoplasmic reticulum stress protein homologous to HSP90, also associates with unassembled immunoglobulin chains, but its interaction is biochemically, kinetically and structurally distinct from BiP's. We report here that whereas BiP preferentially binds an early disulphide intermediate of light chain and dissociates within a few minutes, GRP94 exclusively binds fully oxidized molecules and dissociates with a half-time of 50 min. These results indicate that GRP94 is itself a chaperone which acts after BiP. SN - 0028-0836 UR - https://www.unboundmedicine.com/medline/citation/7913987/Sequential_interaction_of_the_chaperones_BiP_and_GRP94_with_immunoglobulin_chains_in_the_endoplasmic_reticulum_ L2 - https://doi.org/10.1038/370373a0 DB - PRIME DP - Unbound Medicine ER -