| Literature DB >> 23792244 |
Masayoshi Fukasawa1, Anda Cornea, Oleg Varlamov.
Abstract
Two distinct sets of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) catalyze membrane fusion in the cis-Golgi and trans-Golgi. The mechanism that controls Golgi localization of SNAREs remains largely unknown. Here we tested three potential mechanisms, including vesicle recycling between the Golgi and the endoplasmic reticulum, partitioning in Golgi lipid microdomains, and selective intra-Golgi retention. Recycling rates showed a linear relationship with intra-Golgi mobility of SNAREs. The cis-Golgi SNAREs had higher mobility than intra-Golgi SNAREs, whereas vesicle SNAREs had higher mobility than target membrane SNAREs. The differences in SNARE mobility were not due to preferential partitioning into detergent-resistant membrane microdomains. We propose that intra-Golgi retention precludes entropy-driven redistribution of SNAREs to the endoplasmic reticulum and endocytic compartments.Entities:
Keywords: Dynamic equilibrium; ER; Endoplasmic reticulum; Entropy; Golgi; Golgi tether; Homotypic fusion; Lipid raft; Membrane fusion; Recycling; Retention; SNARE; Vesicle; i-SNARE
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Year: 2013 PMID: 23792244 DOI: 10.1016/j.febslet.2013.06.004
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124