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Titolo:
Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels
Autore:
Martin, PEM; Blundell, G; Ahmad, S; Errington, RJ; Evans, WH;
Indirizzi:
Univ Wales Coll Med, Dept Biochem Med, Cardiff CF14 4XN, S Glam, Wales Univ Wales Coll Med Cardiff S Glam Wales CF14 4XN CF14 4XN, S Glam, Wales
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 21, volume: 114, anno: 2001,
pagine: 3845 - 3855
SICI:
0021-9533(200111)114:21<3845:MPITTA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOUSE MAMMARY-GLAND; X-LINKED DISEASE; PLASMA-MEMBRANE; FLUORESCENT PROTEIN; INTRACELLULAR TRAFFICKING; SELECTIVE PERMEABILITY; HETEROMERIC CONNEXONS; ENDOPLASMIC-RETICULUM; CALCIUM ENVIRONMENTS; LIVING CELLS;
Keywords:
connexin-fluorescent protein chimera; gap junction; trafficking pathways;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
62
Recensione:
Indirizzi per estratti:
Indirizzo: Martin, PEM Univ Wales Coll Med, Wales Heart Res Inst, Dept Radiol, Heath Pk, Cardiff CF14 4XN, S Glam, Wales Univ Wales Coll Med Heath Pk Cardiff S Glam Wales CF14 4XN les
Citazione:
P.E.M. Martin et al., "Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels", J CELL SCI, 114(21), 2001, pp. 3845-3855

Abstract

The assembly of gap junctions was investigated in mammalian cells expressing connexin (Cx) 26, 32 and 43 fused to green, yellow or cyan fluorescent proteins (GFP, YFP, CFP). Targeting of Cx32-CFP and 43-GFP to gap junctions and gap junctional communication was inhibited in cells treated with Brefeldin A, a drug that disassembles the Golgi. However gap junctions constructed of Cx26-GFP were only minimally affected by Brefeldin A. Nocodazole, a microtubule disruptor, had little effect on the assembly of Cx43-GFP gap junctions, but perturbed assembly of Cx26-GFP gap junctions. Co-expression of Cx26-YFP and Cx32-CFP in cells treated with Brefeldin A resulted in assemblyof gap junctions constructed of Cx26-YFP. Two amino acids that distinguishCx26 from Cx32 in transmembrane domains were mutated in Cx32 to investigate underlying mechanisms determining trafficking routes to gap junctions. One mutation, Cx32I28L, conferred on it partial Cx26-like trafficking properties as well the posttranslational membrane insertion characteristics of Cx26, suggesting that a key determinant regulating trafficking was present in the first transmembrane domain. The results provide a protein trafficking basis for specifying and regulating connexin composition of gap junctions and thus selectivity of intercellular signaling, with Cx32 and 43 traffickingthrough the secretory pathway and Cx26 also following an alternative pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 12:37:43