Article
Critical role of the first transmembrane domain of Cx26 in regulating oligomerization and function.
Molecular biology of the cell - 1 Sept 2012
Jara Oscar, Acuña Rodrigo, García Isaac E, Maripillán Jaime, Figueroa Vania, Sáez Juan C, Araya-Secchi Raúl, Lagos Carlos F, Pérez-Acle Tomas, Berthoud Viviana M, Beyer Eric C, Martínez Agustín D
Abstract excerpt
To identify motifs involved in oligomerization of the gap junction protein Cx26, we studied individual transmembrane (TM) domains and the full-length protein. Using the TOXCAT assay for interactions of isolated TM α-helices, we found that TM1, a Cx26 pore domain, had a strong propensity to homodimerize. We identified amino acids Val-37-Ala-40 (VVAA) as the TM1 motif required for homodimerization. Two...
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