ArticleMolecular biology of the cell1998
A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 130 citations in OpenAlex.
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- A selectivity filter in the ER membrane protein complex limits protein misinsertion at the ER.The Journal of cell biology · 2023Article
- MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging inInternational journal of molecular sciences · 2023Article
- Go your own way: membrane-targeting sequences.Plant physiology · 2021Article
- Extracellular anti-angiogenic proteins augment an endosomal protein trafficking pathway to reach mitochondria and execute apoptosis in HUVECs.Cell death and differentiation · 2018Article
- Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells.Journal of cell science · 2017Article
- Targeting of tail-anchored membrane proteins to subcellular organelles in Toxoplasma gondii.Traffic (Copenhagen, Denmark) · 2017Article
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- Novel synaptobrevin-1 mutation causes fatal congenital myasthenic syndrome.Annals of clinical and translational neurology · 2017Article
- An Interactome-Centered Protein Discovery Approach Reveals Novel Components Involved in Mitosome Function and Homeostasis in Giardia lamblia.PLoS pathogens · 2016Article
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- A new pathway for mitochondrial quality control: mitochondrial-derived vesicles.The EMBO journal · 2014Review
- Loss of PiT-1 results in abnormal endocytosis in the yolk sac visceral endoderm.Mechanisms of development · 2014Article
- NFAT1 and NFAT3 cooperate with HDAC4 during regulation of alternative splicing of PMCA isoforms in PC12 cells.PloS one · 2014Article
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- Overexpression of ryanodine receptor type 1 enhances mitochondrial fragmentation and Ca2+-induced ATP production in cardiac H9c2 myoblasts.American journal of physiology. Heart and circulatory physiology · 2013Article
- Tail-anchored PEX26 targets peroxisomes via a PEX19-dependent and TRC40-independent class I pathway.The Journal of cell biology · 2013Article
- A C-Terminal Transmembrane Anchor Targets the Nuage-Localized Spermatogenic Protein Gasz to the Mitochondrial Surface.ISRN cell biology · 2013Article
- VAMP1 mutation causes dominant hereditary spastic ataxia in Newfoundland families.American journal of human genetics · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Screening of a library derived from primary human endothelial cells revealed a novel human isoform of vesicle-associated membrane protein-1 (VAMP-1), a protein involved in the targeting and/or fusion of transport vesicles to their target membrane. We have termed this novel isoform VAMP-1B and designated the previously described isoform VAMP-1A. VAMP-1B appears to be an alternatively spliced form of VAMP-1. A similar rat splice variant of VAMP-1 (also termed VAMP-1B) has recently been reported. Five different cultured cell lines, from different lineages, all contained VAMP-1B but little or no detectable VAMP-1A mRNA, as assessed by PCR. In contrast, brain mRNA contained VAMP-1A but no VAMP-1B. The VAMP-1B sequence encodes a protein identical to VAMP-1A except for the carboxy-terminal five amino acids. VAMP-1 is anchored in the vesicle membrane by a carboxy-terminal hydrophobic sequence. In VAMP-1A the hydrophobic anchor is followed by a single threonine, which is the carboxy-terminal amino acid. In VAMP-1B the predicted hydrophobic membrane anchor is shortened by four amino acids, and the hydrophobic sequence is immediately followed by three charged amino acids, arginine-arginine-aspartic acid. Transfection of human endothelial cells with epitope-tagged VAMP-1B demonstrated that VAMP-1B was targeted to mitochondria whereas VAMP-1A was localized to the plasma membrane and endosome-like structures. Analysis of C-terminal mutations of VAMP-1B demonstrated that mitochondrial targeting depends both on the addition of positive charge at the C terminus and a shortened hydrophobic membrane anchor. These data suggest that mitochondria may be integrated, at least at a mechanistic level, to the vesicular trafficking pathways that govern protein movement between other organelles of the cell.
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