About: Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain

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About: Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain
Creator	Sato, Ken Sato, Miyuki Nakano, Akihiko
Source	PMC
abstract	Yeast Sec12p is a type II transmembrane protein in the ER, which is essential for the formation of transport vesicles. From biochemical and morphological lines of evidence, we have proposed that Sec12p is localized to the ER by two mechanisms: static retention in the ER and dynamic retrieval from the early Golgi compartment. We have also shown that Rer1p, a membrane protein in the Golgi, is required for correct localization of Sec12p. In the present study, we have performed a systematic analysis to determine the ER localization signals in Sec12p corresponding to these two mechanisms. Both the transmembrane domain (TMD) and the NH2-terminal cytoplasmic domain of Sec12p show the ability to localize the protein to the ER. The effect of the TMD is potent and sufficient by itself for the ER localization and is strongly dependent on Rer1p. On the other hand, the cytoplasmic domain shows a moderate ER-localization capability which is independent of Rer1p. The rate of mannosyl modification has been measured to distinguish between retention and retrieval. The cytoplasmic domain significantly delays the transport from the ER to the cis-Golgi. In contrast, the TMD shows only a subtle retardation in the transport from the ER to the cis-Golgi but strictly prevents the transport beyond there. From these observations, we conclude that the TMD mainly acts as the retrieval signal and the cytoplasmic domain contains the retention signal. This study not only supports the two-mechanisms hypothesis but also provides powerful tools to dissect the two.
has issue date	1996-07-02(xsd:dateTime)
bibo:pmid	8707815
has license	cc-by-nc-sa
sha1sum (hex)	2a771153af1b6fd5e71dc23f5db7c83bb5a3f231
resource representing a document's title	Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain
has PubMed Central identifier	PMC2120888
has PubMed identifier	8707815
schema:publication	J Cell Biol
resource representing a document's body	covid:2a771153af1b6fd5e71dc23f5db7c83bb5a3f231#body_text
is schema:about of	named entity 'YEAST' named entity 'Domain' named entity 'Transmembrane' named entity 'DEPENDENT' named entity 'CYTOPLASMIC DOMAIN' named entity 'RETRIEVAL' named entity 'TRANSMEMBRANE DOMAIN' named entity 'ENDOPLASMIC RETICULUM LOCALIZATION' named entity 'TYPE II' named entity 'IS A' named entity 'TRANSMEMBRANE' named entity 'MECHANISMS' named entity 'RETENTION' named entity 'INDEPENDENT' named entity 'DSDm' named entity 'a-factor' named entity 'S. Tanaka' named entity 'DSDm' named entity 'dissection' named entity 'homology' named entity 'SDS' named entity 'fluorescein' named entity 'Immunofluorescence microscopy' named entity 'Golgi apparatus' named entity 'immunoprecipitated' named entity 'Golgi' named entity 'protease' named entity 'subcloned' named entity 'antibody' named entity 'Golgi' named entity 'Journal of Cell Biology' named entity 'PCR' named entity 'NH2-terminal' named entity 'wild-type' named entity 'NH2-terminal' named entity 'ER retention' named entity 'mutant proteins' named entity 'Golgi' named entity 'Lys' named entity 'membrane protein' named entity 'staining' named entity 'a-factor' named entity 'cytoplasmic domain' named entity 'thiocyanate' named entity 'cytoplasmic domain' named entity 'Tokyo' named entity 'antibody' named entity 'image scanning' named entity 'Cosson' named entity 'ER membrane' named entity 'steady state' named entity 'amino acid residues' named entity 'Glu' named entity 'SDDm' named entity 'secretion' named entity 'chimeric protein' named entity 'codon' named entity 'Immunofluorescence microscopy' named entity 'fusion protein' named entity 'cis-Golgi' named entity 'proteolytic activities' named entity 'Golgi' named entity 'yeast' named entity 'dideoxy method' named entity 'Escherichia coli' named entity 'c/s' named entity 'structural motifs' named entity 'COOH' named entity 'a-factor' named entity 'amino acids' named entity 'protein' named entity 'antibodies' named entity 'Sambrook' named entity 'SDDm' named entity 'XbaI' named entity 'membrane-bound organelles' named entity 'codon' named entity 'primers' named entity 'yeast' named entity 'cis' named entity 'biochemical'

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