Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2.

Archer, Branch T.; Özçelık, Tayfun; Jahn, Reinhard; Francke, Uta; Südhof, Thomas C.

doi:10.1016/s0021-9258(17)44898-8

Cited by 133 publications

(12 citation statements)

References 26 publications

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“…Screening a library constructed from the cDNA of differentiated HL-60 cells for VAMP-2, we obtained a single clone (termed M40D1). This sequence was 848 bp in length, containing an open reading frame, and was identical (in the coding sequence) to that reported for human VAMP-2, which is encoded in five exons (24). Our 848-bp sequence had 28 bp of 5′-untranslated sequence as well as 427 bp of 3′-untranslated sequence, that was rich in poly-A.…”

Section: Vamp-2supporting

confidence: 64%

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et al. 2001

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Degranulation and membrane fusion by neutrophils are essential to host defense. We sought homologues of neuron-specific fusion proteins in human neutrophils and in their precursors, the promyelocytic cell line HL-60. We screened a differentiated HL-60 library and obtained an 848 bp sequence with a 351 bp open reading frame, identical to that published for human VAMP-2 and including 5' and 3' untranslated regions. RNA from HL-60 cells during differentiation into the neutrophil lineage was subjected to Northern blot analysis. which revealed a transcript of approximately 1050 bp at all stages of differentiation. The amount of these transcripts increased approximately threefold during differentiation, a finding confirmed by quantitative RT-PCR. We also detected mRNA for VAMP-2 in human neutrophils and monocytes using RT-PCR. In like fashion, transcripts of syntaxin-4, another fusion protein, were recovered from a neutrophil cDNA library. As with VAMP-2, expression of syntaxin-4 (determined by Northern blots) also increased, but by only 50%, during differentiation of HL-60 cells. These studies demonstrate that neutrophils and their progenitors possess mRNA for the fusion proteins VAMP-2 and syntaxin-4, and that their transcription increases during differentiation, concurrent with the functional maturation of myeloid cells.

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Section: Vamp-2supporting

confidence: 64%

“…We obtained a single clone (designated M40D1), 848 bp long, containing an open reading frame with the entire coding region for human VAMP-2, with both 5′-and 3′-untranslated regions. This sequence was identical to that published for the human neuronal protein and contained portions of all five published exons (24).…”

Section: Vamp-2mentioning

confidence: 62%

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et al. 2001

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“…Two types of mechanism have been proposed: those that increase availability of glutamate and those that increase the postsynaptic response to a fixed level of glutamate release (for review see Kullmann, 2003). The vesicular protein VAMP (synaptobrevin) (Archer et al, 1990;Baumert et al, 1989;Elferink et al, 1989;Sollner et al, 1993) is required for vesicle exocytosis (Schoch et al, 2001;Sudhof, 1995) and is proteolytically cleaved by TeNT (Link et al, 1992;Schiavo et al, 1992). The light chain of TeNT is unable to cross the plasma membrane and has been used in our experiments to prevent exocytosis in the postsynaptic neuron.…”

Section: Discussionmentioning

confidence: 99%

State-Dependent Mechanisms of LTP Expression Revealed by Optical Quantal Analysis

Ward

McGuinness

Akerman

et al. 2006

Neuron

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The expression mechanism of long-term potentiation (LTP) remains controversial. Here we combine electrophysiology and Ca(2+) imaging to examine the role of silent synapses in LTP expression. Induction of LTP fails to change p(r) at these synapses but instead mediates an unmasking process that is sensitive to the inhibition of postsynaptic membrane fusion. Once unmasked, however, further potentiation of formerly silent synapses leads to an increase in p(r). The state of the synapse thus determines how LTP is expressed.

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“…ERS-24 is also homologous to a number of other putative v-SNAREs (18-28% sequence identity and 40-50% similarity). Homologous v-SNAREs include the SAR1 gene product of Arabidopsis thaliana (Schena and Davis, 1992) (no relation to the yeast GTPase also termed SAR1 [Barlowe et al, 1993]); p26/Ykt6, a prenylated SNARE in yeast (Søgaard et al, 1994); the yeast proteins Snc1p and Snc2p (Protopopov et al, 1993); the mammalian cellubrevin (McMahon et al, 1993); and the neuronal synaptobrevins/VAMPs 1 and 2 from many different sources (Trimble et al, 1988;Elferink et al, 1989;Baumert et al, 1989;Archer et al, 1990;Südhof et al, 1989). Interestingly, most of the homology resides within the carboxy-terminal onethird of these proteins (amino acid residues 130-190), while the amino-terminal halves of these proteins are widely divergent.…”

Section: Ers-24 Is Homologous To Sec22p and Rsec22mentioning

confidence: 99%

ERS-24, a Mammalian v-SNARE Implicated in Vesicle Traffic between the ER and the Golgi

Paek

Orci

Ravazzola

et al. 1997

The Journal of Cell Biology

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We report the identification and characterization of ERS-24 (Endoplasmic Reticulum SNARE of 24 kD), a new mammalian v-SNARE implicated in vesicular transport between the ER and the Golgi. ERS24 is incorporated into 20S docking and fusion particles and disassembles from this complex in an ATP-dependent manner. ERS-24 has significant sequence homology to Sec22p, a v-SNARE in Saccharomyces cerevisiae required for transport between the ER and the Golgi. ERS-24 is localized to the ER and to the Golgi, and it is enriched in transport vesicles associated with these organelles.

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Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2.

Cited by 133 publications

References 26 publications

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Untitled

State-Dependent Mechanisms of LTP Expression Revealed by Optical Quantal Analysis

ERS-24, a Mammalian v-SNARE Implicated in Vesicle Traffic between the ER and the Golgi

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