About: Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues

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About: Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues
Creator	Roberts, Christopher Stevens, Tom Nothwehr, Steven
Source	PMC
abstract	The mechanism by which yeast dipeptidyl aminopeptidase (DPAP) A, type II integral membrane protein, is retained in the late Golgi apparatus has been investigated. Prior work demonstrated that the 118-amino acid cytoplasmic domain is both necessary and sufficient for Golgi retention and that mutant or overexpressed DPAP A no longer retained in the Golgi was delivered directly to the vacuolar membrane (Roberts, C. J., S. F. Nothwehr, and T. H. Stevens. 1992. J. Cell Biol. 119:69-83). Replacement of the DPAP A transmembrane domain with a synthetic hydrophobic sequence did not affect either Golgi retention of DPAP A or vacuolar delivery of the retention-defective form of DPAP A. These results indicate that the DPAP A transmembrane domain is not involved in either Golgi retention or targeting of this membrane protein. A detailed mutational analysis of the cytoplasmic domain of DPAP A indicated that the most important elements for retention were within the eight residue stretch 85-92. A 10-amino acid region from DPAP A (81- 90) was sufficient for Golgi retention of alkaline phosphatase, a type II vacuolar membrane protein. Detailed mutational analysis within this 10-amino acid sufficient region demonstrated that a Phe-X-Phe-X-Asp motif was absolutely required for efficient retention. The efficiency of Golgi retention via the DPAP A signal could be diminished by overexpression of wild type but not retention-defective versions of Kex2p, another late Golgi membrane protein, suggesting that multiple Golgi membrane proteins may be retained by a common machinery. These results imply a role for a cytoplasmic signal involving aromatic residues in retention of late Golgi membrane proteins in the yeast Saccharomyces cerevisiae.
has issue date	1993-06-02(xsd:dateTime)
bibo:pmid	8509444
has license	cc-by-nc-sa
sha1sum (hex)	05b5ca303bd262f2a8e7d9d05d203f023867d0ed
resource representing a document's title	Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues
has PubMed Central identifier	PMC2119699
has PubMed identifier	8509444
schema:publication	J Cell Biol
resource representing a document's body	covid:05b5ca303bd262f2a8e7d9d05d203f023867d0ed#body_text
is schema:about of	named entity 'PROTEIN RETENTION' named entity 'DIPEPTIDYL AMINOPEPTIDASE' named entity 'AROMATIC' named entity 'RETAINED' named entity 'CONTAINING' named entity 'GOLGI APPARATUS' named entity 'CYTOPLASMIC' named entity 'AMINOPEPTIDASE A' named entity 'MEMBRANE PROTEIN' named entity 'MEM' named entity 'SIGNAL' named entity 'YEAST' named entity 'DIPEPTIDYL AMINOPEPTIDASE' named entity 'TYPE II' named entity 'INTEGRAL' named entity 'MECHANISM' named entity 'YEAST' named entity 'yeast' named entity 'glycosylated' named entity 'tyrosine' named entity 'plasma membrane' named entity '7.2' named entity 'Golgi' named entity 'wild-type' named entity 'vacuolar' named entity 'plasmid' named entity 'plasma membrane' named entity 'cytoplasmic domain' named entity 'Golgi' named entity 'urea' named entity 'Kex2p' named entity 'aromatic residues' named entity 'Phe' named entity 'endogenous' named entity 'amino acid sequence' named entity 'SDS' named entity 'Biotechnology' named entity 'transmembrane domain' named entity 'membrane protein' named entity 'Kex2p' named entity 'EDTA' named entity 'type II' named entity 'Kex2p' named entity 'nucleotides' named entity 'Golgi' named entity 'membrane protein' named entity 'amino acid' named entity 'Mutagenic' named entity 'silent mutation' named entity 'antigens' named entity 'A87' named entity 'transmembrane domains' named entity 'Golgi' named entity 'Kex2p' named entity 'Golgi' named entity 'mutagenesis' named entity 'Yeast' named entity 'University of Oregon' named entity 'V-ATPase' named entity 'AgA' named entity 'motif' named entity 'CEN' named entity 'Golgi apparatus' named entity 'plasmids' named entity 'mammalian cells' named entity 'coliphage' named entity 'restriction digest' named entity 'immunofluorescence microscopy' named entity 'vacuolar' named entity 'yeast' named entity 'yeast cells' named entity 'vacuolar' named entity 'cation' named entity 'yeast' named entity 'cytoplasmic domain' named entity 'COOH terminus' named entity 'rhodamine' named entity 'yeast' named entity 'yeast' named entity 'organelle' named entity 'SDS'

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