Journal
CARDIOVASCULAR RESEARCH
Volume 62, Issue 2, Pages 256-267Publisher
OXFORD UNIV PRESS
DOI: 10.1016/j.cardiores.2003.12.021
Keywords
proteasome; lysosome; half-life; intercellular communication; connexin; gap junction
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Funding
- NHLBI NIH HHS [R01 HL045466] Funding Source: Medline
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Gap junctional proteins, connexins, and gap junctional plaques are short-lived. Three pathways for their degradation have been proposed: (1) misfolded/abnormally oligomerized connexins are retrogradely translocated and degraded by the proteasome through endoplasmic reticulum-associated degradation; (2) connexins (as monomers or oligomers) may traffic directly from an early secretory compartment to the lysosome for degradation without reaching the plasma membrane; (3) connexins within gap junction plaques are degraded by the lysosome after endocytotic internalization. Degradation of gap junction plaques is proteasome-dependent in some cell types. Degradation may be regulated by ubiquitinylation, phosphorylation, or polypeptide domains that act as sorting signals. (C) 2004 European Society of Cardiology. Published by Elsevier B.V. All rights reserved.
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