p115 SNAREs a vesicle

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p115 SNAREs a vesicle

p115 SNAREs a vesicle protein known to tether vesicles during intra-Golgi trafficking also ensures their correct docking, according to new results from Shorter et al. (page 45). This provides the first link between the long-range process of tethering and the short-range process of docking. Vesicle transfer consists of four successive reactions: vesicle formation, tethering, docking, and fusion....

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Commentary SNAREs and regulated vesicle exocytosis

Synaptic vesicle exocytosis—the basis for neurotransmitter release at nerve terminals—is at the heart of nervous system functioning. The molecular analysis of this special form of exocytosis was recently greatly stimulated by the finding that the key molecules in various intracellular vesicular transport steps, including neurotransmitter release, are conserved from yeast to man (1–3). Prompted ...

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The specificity of vesicle trafficking: coat proteins and SNAREs.

Proteins that are destined for the secretory system usually begin their journey at the endoplasmic reticulum (ER), where proteins are translocated across the ER membrane into the lumen, before being selectively removed from the ER and packaged as cargo into transport vesicles bound for the stacks of the Golgi complex. Protein cargo then passes through the Golgi to the trans -Golgi network (TGN)...

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The role of non-canonical SNAREs in synaptic vesicle recycling

An increasing number of studies suggest that distinct pools of synaptic vesicles drive specific forms of neurotransmission. Interspersed with these functional studies are analyses of the synaptic vesicle proteome which have consistently detected the presence of so-called "non-canonical" SNAREs that typically function in fusion and trafficking of other subcellular structures within the neuron. T...

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Binding of the vesicle docking protein p115 to the GTPase Rab1b regulates membrane recruitment of the COPI vesicle coat

Membrane recruitment of the COPI vesicle coat is fundamental to its function and contributes to compartment identity in the early secretory pathway. COPI recruitment is triggered by guanine nucleotide exchange activating the Arf1 GTPase, but the key exchange factor, GBF1, is a peripheral membrane component whose membrane association is dependent on another GTPase, Rab1. Inactive Rab GTPases are...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 2002

ISSN: 1540-8140,0021-9525

DOI: 10.1083/jcb1571iti5