The large external domain is sufficient for the correct sorting of secreted or chimeric influenza virus hemagglutinins in polarized monkey kidney cells.
The large external domain is sufficient for the correct sorting of secreted or chimeric influenza virus hemagglutinins in polarized monkey kidney cells.
复制标题
大的外部结构域足以正确分选极化猴肾细胞中分泌的或嵌合的流感病毒血凝素。
DOI:
10.1083/jcb.104.3.769
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发表时间:
1987
期刊:
影响因子:
--
通讯作者:
Rodriguez-Boulan,E
中科院分区:
文献类型:
--
作者:
Roth,MG;Gundersen,D;Patil,N;Rodriguez-Boulan,E
MA104. 11 rhesus kidney cells express several characteristics of polarized epithelial cells, including the formation of" domes" on impermeable substrates, the establishment of a transmonolayer electrical resistance when grown on collagen gels, the polarized maturation of influenza and vesicular stomatitis viruses, and the expression of the glycoproteins of those viruses at a single surface domain. The polarized expression of the influenza virus hemagglutinin (HA) is maintained in MA104. 11 cells infected with SV40-derived vectors carrying a cDNA gene for either the wild-type influenza virus HA, a truncated HA gene encoding a secreted form of HA (HA~ c), or a chimeric gene encoding a hybrid protein with the external domain of the HA and the transmembrane and cytoplasmic domains of the vesicular stomatitis virus G protein (HAG). Thus, the recognition event separating glycoproteins, such as HA, destined for the apical surface from proteins, such as G, destined for the basolateral membranes involves features of the external domains of the proteins. The transmembrane and cytoplasmic domains of HA have no role in this process.UKARVOTIC cells direct a complex internal traffic of proteins moving from common sites of synthesis to separate final destinations. In polarized epithelial cells an aspect of this traffic is the transport of secreted and membrane-bound proteins to structurally distinct domains of the plasmalemma. These surface domains, delimited by the junctional complexes of the zonula occludentes, each contain unique sets of proteins required for their functional specialization (reviewed by Rodriguez-Boulan, 1983a; Simons and Fuller, 1985). Obviously, there are mechanisms for the recognition, sorting, and directional transport of these sets of proteins.