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Reticulon 1‐C/neuroendocrine‐specific protein‐C interacts with SNARE proteins
Author(s) -
Steiner Pascal,
Kulangara Karina,
Sarria J. C. Floyd,
Glauser Liliane,
Regazzi Romano,
Hirling Harald
Publication year - 2004
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2004.02345.x
Subject(s) - endoplasmic reticulum , calreticulin , microbiology and biotechnology , calnexin , syntaxin , biology , exocytosis , snap23 , munc 18 , secretion , immunoprecipitation , syntaxin 3 , snare complex , membrane protein , vesicle , biochemistry , vesicle associated membrane protein 8 , synaptic vesicle , membrane , gene
Reticulons are proteins of neuroendocrine cells localized primarily to the endoplasmic reticulum membrane. Despite their implication in cellular processes like apoptosis or axonal regeneration, their intracellular molecular function is still largely unknown. Here, we show that reticulon 1‐C can be detected in a protein complex of 150–200 kDa, and that a number of soluble N‐ethylmaleimide‐sensitive factor attachment protein receptor (SNARE) proteins, i.e. syntaxin 1, syntaxin 7, syntaxin 13 and VAMP2, can be co‐immunoprecipitated with reticulon 1‐C. Moreover, it localizes to a nocodazole‐sensitive, but calreticulin‐negative domain of the endoplasmic reticulum. Finally, overexpression in PC12 cells of a reticulon 1‐C fragment which binds to SNAREs, significantly enhances human growth hormone secretion. These results suggest that reticulons are involved in vesicle trafficking events, including regulated exocytosis.