Lectins and protein traffic early in the secretory pathway.
Biochem Soc Symp
; (69): 73-82, 2002.
Article
em En
| MEDLINE
| ID: mdl-12655775
ABSTRACT
Lectins of the early secretory pathway are involved in selective transport of newly synthesized glycoproteins from the endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). The most prominent cycling lectin is the mannose-binding type I membrane protein ERGIC-53 (ERGIC protein of 53 kDa), a marker for the ERGIC, which functions as a cargo receptor to facilitate export of an increasing number of glycoproteins with different characteristics from the ER. Two ERGIC-53-related proteins, VIP36 (vesicular integral membrane protein 36) and a novel ERGIC-53-like protein, ERGL, are also found in the early secretory pathway. ERGL may act as a regulator of ERGIC-53. Studies of ERGIC-53 continue to provide new insights into the organization and dynamics of the early secretory pathway. Analysis of the cycling of ERGIC-53 uncovered a complex interplay of trafficking signals and revealed novel cytoplasmic ER-export motifs that interact with COP-II coat proteins. These motifs are common to type I and polytopic membrane proteins including presenilin 1 and presenilin 2. The results support the notion that protein export from the ER is selective.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Lectinas de Ligação a Manose
/
Lectinas
/
Proteínas de Membrana
Limite:
Animals
Idioma:
En
Revista:
Biochem Soc Symp
Ano de publicação:
2002
Tipo de documento:
Article
País de afiliação:
Suíça