9651318

Source:http://linkedlifedata.com/resource/pubmed/id/9651318

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0014139, umls-concept:C0086597, umls-concept:C0169582, umls-concept:C0205378, umls-concept:C0599682, umls-concept:C1514562
pubmed:issue	28
pubmed:dateCreated	1998-8-6
pubmed:abstractText	Specific transport proteins mediate the packaging of neurotransmitters into secretory vesicles and consequently require targeting to the appropriate intracellular compartment. To identify residues in the neuron-specific vesicular monoamine transporter (VMAT2) responsible for endocytosis, we examined the effect of amino (NH2-) and carboxyl (COOH-)-terminal mutations on steady state distribution and internalization. Deletion of a critical COOH-terminal domain sequence (AKEEKMAIL) results in accumulation of VMAT2 at the plasma membrane and a 50% reduction in endocytosis. Site-directed mutagenesis shows that replacement of the isoleucine-leucine pair within this sequence by alanine-alanine alone reduces endocytosis by 50% relative to wild type VMAT2. Furthermore, the KEEKMAIL sequence functions as an internalization signal when transferred to the plasma membrane protein Tac, and the mutation of the isoleucine-leucine pair also abolishes internalization of this protein. The closely related vesicular acetylcholine transporter (VAChT) contains a similar di-leucine sequence within the cytoplasmic COOH-terminal domain that when mutated results in accumulation of VAChT at the plasma membrane. The VAChT di-leucine sequence also confers internalization when appended to two other proteins and in one of these chimeras, conversion of the di-leucine sequence to di-alanine reduces the internalization rate by 50%. Both VMAT2 and VAChT thus use leucine-based signals for efficient endocytosis and as such are the first synaptic vesicle proteins known to use this motif for trafficking.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2985121R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholine, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Leucine, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides, http://linkedlifedata.com/resource/pubmed/chemical/Neurotransmitter Agents, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Acetylcholine Transport..., http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Biogenic Amine Transport..., http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Monoamine Transport..., http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
pubmed:status	MEDLINE
pubmed:month	Jul
pubmed:issn	0021-9258
pubmed:author	pubmed-author:EdwardsR HRH, pubmed-author:KramerJ IJI, pubmed-author:LieII, pubmed-author:RaoR HRH, pubmed-author:WaitesCC
pubmed:issnType	Print
pubmed:day	10
pubmed:volume	273
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	17351-60
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:9651318-Acetylcholine, pubmed-meshheading:9651318-Amino Acid Sequence, pubmed-meshheading:9651318-Animals, pubmed-meshheading:9651318-COS Cells, pubmed-meshheading:9651318-Carrier Proteins, pubmed-meshheading:9651318-Endocytosis, pubmed-meshheading:9651318-Leucine, pubmed-meshheading:9651318-Membrane Glycoproteins, pubmed-meshheading:9651318-Membrane Proteins, pubmed-meshheading:9651318-Membrane Transport Proteins, pubmed-meshheading:9651318-Molecular Sequence Data, pubmed-meshheading:9651318-Mutagenesis, Site-Directed, pubmed-meshheading:9651318-Neuropeptides, pubmed-meshheading:9651318-Neurotransmitter Agents, pubmed-meshheading:9651318-Sequence Homology, Amino Acid, pubmed-meshheading:9651318-Vesicular Acetylcholine Transport Proteins, pubmed-meshheading:9651318-Vesicular Biogenic Amine Transport Proteins, pubmed-meshheading:9651318-Vesicular Monoamine Transport Proteins, pubmed-meshheading:9651318-Vesicular Transport Proteins
pubmed:year	1998
pubmed:articleTitle	A leucine-based motif mediates the endocytosis of vesicular monoamine and acetylcholine transporters.
pubmed:affiliation	Departments of Neurology and Physiology, Graduate Programs in Neuroscience and Cell Biology, University of California School of Medicine, San Francisco, California 94143-0435, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't