Regular ArticleSNAP-29 Is a Promiscuous Syntaxin-Binding SNARE
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Postsynaptic SNARE Proteins: Role in Synaptic Transmission and Plasticity
2019, NeuroscienceCitation Excerpt :In addition, SNAP-29 contains an N-terminal motif that facilities the interaction with endocytic adaptors and small GTPases like Rab3A (Rotem-Yehudar et al., 2001; Schardt et al., 2009). In contrast with SNAP-25 and SNAP-23, SNAP-29 has been reported to have a widespread expression throughout neurons and to interact with a wide variety of syntaxin isoforms (Steegmaier et al., 1998; Hohenstein and Roche, 2001). SNAP-29 levels in the CNS are low in comparison with its paralogs, however it has been reported that SNAP-29 mRNA expression may be regulated by electrical activity and a single session of electroconvulsive seizures on the rat frontal cortex induced an upregulation of the SNAP-29 messenger in the hippocampus (Elfving et al., 2008).
Finding the Middle Ground for Autophagic Fusion Requirements
2018, Trends in Cell BiologyCitation Excerpt :The silencing of IRGM disrupts the normal colocalization of STX17 with LC3, demonstrating a targeting role for IRGM [9]. SNAP29 is a promiscuous, non-lipid anchored Qbc-SNARE (see Box 1) that donates two coiled-coil domains to the forming SNARE bundle [11]. SNAP29 binds STX17 on the autophagosome and facilitates binding to VAMP8 [6].
Molecular Functions of Glycoconjugates in Autophagy
2016, Journal of Molecular BiologyEstablishment of Two Mouse Models for CEDNIK Syndrome Reveals the Pivotal Role of SNAP29 in Epidermal Differentiation
2016, Journal of Investigative DermatologyCitation Excerpt :SNAP29 belongs to the family of soluble N-ethylmaleimide–sensitive factor attachment protein receptor proteins, which mediate membrane fusion between vesicles and target membranes in eukaryotic cells. The human SNAP29 gene is expressed in many tissues and seems to be involved in a variety of intracellular membrane fusion processes (Hohenstein and Roche, 2001; Steegmaier et al., 1998), among others, in endocytotic recycling and cell motility (Rapaport et al., 2010). The pronounced cutaneous phenotype of CEDNIK syndrome suggests a crucial role of SNAP29 in epidermal differentiation and barrier formation (Sprecher et al., 2005).
Membrane Trafficking in Neuronal Development: Ins and Outs of Neural Connectivity
2016, International Review of Cell and Molecular BiologyThe exocyst subunit Sec6 interacts with assembled exocytic SNARE complexes
2015, Journal of Biological ChemistryCitation Excerpt :Vesicles containing the exocytic Sso1-Sec9 t-SNARE complex can fuse with vesicles containing v-SNAREs other than Snc1/2 (15), and vesicles loaded with the vacuolar t-SNARE complex (Vam3, Vti1, and Vam7) can fuse with vesicles containing non-vacuolar v-SNAREs, including the exocytic/endocytic Snc2 (16). This promiscuity extends to mammalian cells; SNAREs from various intracellular compartments can form stable non-cognate SNARE complexes, suggesting that SNARE complex formation is not the sole determinant of specificity (17–19). Secondly, the localization of Sec9 and Sso1 is not restricted to the yeast bud tips and mother-daughter necks where secretion is occurring.
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