pH-dependent intramolecular binding and structure involving Cx43 cytoplasmic domains

Heather S. Duffy; Paul L. Sorgen; Mark E. Girvin; Phyllis O'Donnell; Wanda Coombs; Steven M. Taffet; Mario Delmar; David C. Spray

doi:10.1074/jbc.M207016200

pH-dependent intramolecular binding and structure involving Cx43 cytoplasmic domains

Heather S. Duffy, Paul L. Sorgen, Mark E. Girvin, Phyllis O'Donnell, Wanda Coombs, Steven M. Taffet, Mario Delmar, David C. Spray

Research output: Contribution to journal › Article › peer-review

151 Scopus citations

Abstract

pH-induced closure of connexin43 (Cx43) channels involves interaction of the Cx43 carboxyl-terminal (Cx43CT) with a separate "receptor" domain. The receptor location and structure and whether the interaction is directly intramolecular are unknown. Here we show resonant mirror technology, enzyme-linked sorbent assays, and nuclear magnetic resonance (NMR) experiments demonstrating pH-dependent binding of Cx43CT to region 119-144 of Cx43 (Cx43L2), which we propose is the receptor. NMR showed that acidification induced α-helical order in Cx43L2, whereas only a minor modification in Cx43CT structure was detected. These data provide the first demonstration of chemically induced structural order and binding between cytoplasmic connexin domains.

Original language	English (US)
Pages (from-to)	36706-36714
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	277
Issue number	39
DOIs	https://doi.org/10.1074/jbc.M207016200
State	Published - Sep 27 2002

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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abstract = "pH-induced closure of connexin43 (Cx43) channels involves interaction of the Cx43 carboxyl-terminal (Cx43CT) with a separate {"}receptor{"} domain. The receptor location and structure and whether the interaction is directly intramolecular are unknown. Here we show resonant mirror technology, enzyme-linked sorbent assays, and nuclear magnetic resonance (NMR) experiments demonstrating pH-dependent binding of Cx43CT to region 119-144 of Cx43 (Cx43L2), which we propose is the receptor. NMR showed that acidification induced α-helical order in Cx43L2, whereas only a minor modification in Cx43CT structure was detected. These data provide the first demonstration of chemically induced structural order and binding between cytoplasmic connexin domains.",

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AU - Duffy, Heather S.

AU - Sorgen, Paul L.

AU - Girvin, Mark E.

AU - O'Donnell, Phyllis

AU - Coombs, Wanda

AU - Taffet, Steven M.

AU - Delmar, Mario

AU - Spray, David C.

PY - 2002/9/27

Y1 - 2002/9/27

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AB - pH-induced closure of connexin43 (Cx43) channels involves interaction of the Cx43 carboxyl-terminal (Cx43CT) with a separate "receptor" domain. The receptor location and structure and whether the interaction is directly intramolecular are unknown. Here we show resonant mirror technology, enzyme-linked sorbent assays, and nuclear magnetic resonance (NMR) experiments demonstrating pH-dependent binding of Cx43CT to region 119-144 of Cx43 (Cx43L2), which we propose is the receptor. NMR showed that acidification induced α-helical order in Cx43L2, whereas only a minor modification in Cx43CT structure was detected. These data provide the first demonstration of chemically induced structural order and binding between cytoplasmic connexin domains.

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pH-dependent intramolecular binding and structure involving Cx43 cytoplasmic domains

Abstract

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