Kin recognition between medial Golgi enzymes in HeLa cells.
Identifieur interne : 000448 ( Pmc/Curation ); précédent : 000447; suivant : 000449Kin recognition between medial Golgi enzymes in HeLa cells.
Auteurs : T. Nilsson ; M H Hoe ; P. Slusarewicz ; C. Rabouille ; R. Watson ; F. Hunte ; G. Watzele ; E G Berger ; G. WarrenSource :
- The EMBO Journal [ 0261-4189 ] ; 1994.
Abstract
The medial Golgi enzymes, N-acetylglucosaminyltransferase I (NAGT I) and mannosidase II (Mann II), and the trans Golgi enzyme, beta-1,4-galactosyltransferase (GalT) were each retained in the endoplasmic reticulum (ER) by grafting on the cytoplasmic tail of the p33 invariant chain. Transient and stable expression of p33/NAGT I in HeLa cells caused relocation of endogenous Mann II to the ER and transient expression of p33/Mann II had a similar effect on endogenous NAGT I. Neither of these endogenous medial enzymes were affected by transient expression of p33/GalT. These data provide strong evidence for kin recognition between medial Golgi enzymes and suggest a role for them in the organization of the Golgi stack.
Url:
PubMed: 8313901
PubMed Central: 394845
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<author><name sortKey="Watzele, G" sort="Watzele, G" uniqKey="Watzele G" first="G" last="Watzele">G. Watzele</name>
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<author><name sortKey="Berger, E G" sort="Berger, E G" uniqKey="Berger E" first="E G" last="Berger">E G Berger</name>
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<front><div type="abstract" xml:lang="en"><p>The medial Golgi enzymes, N-acetylglucosaminyltransferase I (NAGT I) and mannosidase II (Mann II), and the trans Golgi enzyme, beta-1,4-galactosyltransferase (GalT) were each retained in the endoplasmic reticulum (ER) by grafting on the cytoplasmic tail of the p33 invariant chain. Transient and stable expression of p33/NAGT I in HeLa cells caused relocation of endogenous Mann II to the ER and transient expression of p33/Mann II had a similar effect on endogenous NAGT I. Neither of these endogenous medial enzymes were affected by transient expression of p33/GalT. These data provide strong evidence for kin recognition between medial Golgi enzymes and suggest a role for them in the organization of the Golgi stack.</p>
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<aff>Cell Biology Laboratory, Imperial Cancer Research Fund, London, UK.</aff>
<pub-date pub-type="ppub"><day>1</day>
<month>2</month>
<year>1994</year>
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<volume>13</volume>
<issue>3</issue>
<fpage>562</fpage>
<lpage>574</lpage>
<abstract><p>The medial Golgi enzymes, N-acetylglucosaminyltransferase I (NAGT I) and mannosidase II (Mann II), and the trans Golgi enzyme, beta-1,4-galactosyltransferase (GalT) were each retained in the endoplasmic reticulum (ER) by grafting on the cytoplasmic tail of the p33 invariant chain. Transient and stable expression of p33/NAGT I in HeLa cells caused relocation of endogenous Mann II to the ER and transient expression of p33/Mann II had a similar effect on endogenous NAGT I. Neither of these endogenous medial enzymes were affected by transient expression of p33/GalT. These data provide strong evidence for kin recognition between medial Golgi enzymes and suggest a role for them in the organization of the Golgi stack.</p>
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