Dileucine-like motifs in the C-terminal tail of connexin32 control its endocytosis and assembly into gap junctions
RGD motif
DOI:
10.1242/jcs.207340
Publication Date:
2018-01-20T01:35:15Z
AUTHORS (4)
ABSTRACT
Defects in assembly of gap junction-forming proteins, called connexins (Cxs), are observed a variety cancers. Connexin32 (Cx32; also known as GJB1) is expressed by the polarized cells epithelia. We discovered two dileucine-based motifs, which govern intracellular sorting and endocytosis transmembrane C-terminal tail Cx32 explored their role regulating its abilities pancreatic prostate cancer cells. One motif, designated LI, was located near juxtamembrane domain, whereas other, LL, distally. non-canonical LR, tail. Our results showed that rendering these motifs non-functional had no effect on Cx32. However, LL or LR motif nonfunctional enhanced formation junctions inhibiting clathrin-mediated pathway. Rendering LI inhibited junction augmenting via motifs. studies have defined distinct roles ability.This article has an associated First Person interview with first author paper.
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