ER-resident G i2 protein controls sar1 translocation onto the ER during budding of transport vesicles

Journal of Cellular Biochemistry

Volumn 112, Issue 9, 2011, Pages 2250-2256

  Nakagawa, Hiroshi ^a   Umadome, Haruka ^a   Miyazaki, Shuichi ^b   Tanaka, Katsuhiro ^a   Nishimura, Kazuhiko ^a   Komori, Masayuki ^a   Matsuo, Saburo ^a  

^a Osaka City University   (Japan)

^b TOHO UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

ER resident heterotrimeric G protein; ER to Golgi transport; Mastoparan; Pertussis toxin; Sar1

Indexed keywords

ENDOPLASMIC RETICULUM RESIDENT HETEROTRIMERIC GI2 PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); MASTOPARAN; MASTOPARAN 7; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; PERTUSSIS TOXIN; PROTEIN; SAR1 PROTEIN; UNCLASSIFIED DRUG; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; ISOQUINOLINE DERIVATIVE; MAS7 PROTEIN, SYNTHETIC; MONOMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; N (2 (4 BROMOCINNAMYLAMINO)ETHYL) 5 ISOQUINOLINESULFONAMIDE; N-(2-(4-BROMOCINNAMYLAMINO)ETHYL)-5-ISOQUINOLINESULFONAMIDE; PEPTIDE; PROTEIN KINASE INHIBITOR; SAR1 PROTEIN, RAT; SULFONAMIDE;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CELL BUDDING; CYTOSOL; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM TO GOLGI TRANSPORT; GOLGI COMPLEX; MALE; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; RAT; TRANSPORT AND BINDING PHENOMENA; TRANSPORT VESICLE; WESTERN BLOTTING; ANIMAL; CELL CULTURE; CELL FRACTIONATION; CYTOLOGY; DRUG POTENTIATION; LIVER; LIVER CELL; METABOLISM; MICROSOME; PROTEIN BINDING; PROTEIN TRANSPORT; RABBIT; SPRAGUE DAWLEY RAT;

ANIMALS; CELL FRACTIONATION; CELLS, CULTURED; ENDOPLASMIC RETICULUM; GTP-BINDING PROTEIN ALPHA SUBUNIT, GI2; GUANOSINE 5'-O-(3-THIOTRIPHOSPHATE); HEPATOCYTES; ISOQUINOLINES; LIVER; MALE; MICROSOMES; MONOMERIC GTP-BINDING PROTEINS; PEPTIDES; PERTUSSIS TOXIN; PROTEIN BINDING; PROTEIN KINASE INHIBITORS; PROTEIN TRANSPORT; RABBITS; RATS; RATS, SPRAGUE-DAWLEY; SULFONAMIDES; TRANSPORT VESICLES;

EID: 80051829494     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.23142     Document Type: Article

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