Sorting of Ion Pumps in Polarized Epithelial Cells. a
Sorting of Ion Pumps in Polarized Epithelial Cells. a
复制标题
极化上皮细胞中离子泵的分类。
DOI:
--
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发表时间:
1997
影响因子:
5.2
通讯作者:
Michael J. Caplan
中科院分区:
文献类型:
--
作者:
L. Dunbar;D. Roush;N. Courtois;T. Muth;C. Gottardi;V. Rajendran;J. Geibel;M. Kashgarian;Michael J. Caplan
The physiologic functions of a P-type ATPase are determined not only by its catalytic and regulatory properties but also by its distribution among a cell's various membranous compartments. With polarized epithelial cells that mediate vectorial ion fluxes, the restriction of P-type ion pumps to one or the other distinct domains of the plasmalemma in large measure determines the parent tissue's solute and fluid transport capacities. The biologic significance of these anisotropic distributions is well illustrated by the mechanisms through which the Na,K-ATPase drives the majority of active epithelial secretory and absorptive processes.] In most epithelial cells, the Na,K-ATPase is restricted to the basolateral plasmalemmal domain.2 This membrane surface rests on the epithelial basement membrane, is in contact with the extracellular fluid compartment, and is involved in extensive contacts with neighboring epithelial cells. The basolateral membrane is separated by tight junctions from the apical plasmalemma, which generally confronts a compartment that is topologically continuous with the extracorporeal space. The nonequilibrium ion distributions generated by the sodium pump are exploited by secondary active transport systems to drive uphill secretory and absorptive fluxes. By expressing different classes of transport systems and restricting their distributions to one or the other surface compartment, epithelial cells can use the basolateral population of the Na,K-ATPase to catalyze a remarkably diverse array of unidirectional transport processes. To achieve polarized distribution of P-type ATPase proteins, epithelial cells must be able to target newly synthesized ion pumps to the correct membrane surfaces and to retain them there following their delivery. To participate in these sorting functions, P-type ATPase subunit polypeptides must encode information within their structures that specify their sites of ultimate functional residence. Furthermore, machinery within the epithelial cell must be able to recognize this information and act on its messages3 Efforts to understand the nature of these sorting signals and of the cellular components that interpret them have largely relied on the extensive homology that relates the members of the P-type ATPase family. This high degree of structural
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DOI:
10.1042/bj2310641
发表时间:
1985
期刊:
The Biochemical journal
影响因子:
--
作者:
Hirst,BH;Forte,JG
通讯作者:
Forte,JG
DOI:
--
发表时间:
1994
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Thomas,DC;Roth,MG
通讯作者:
Roth,MG
影响因子:
18.2
作者:
Rabon,EC;Reuben,MA
通讯作者:
Reuben,MA
影响因子:
29.4
作者:
Smolka,A;Weinstein,WM
通讯作者:
Weinstein,WM
影响因子:
56.9
作者:
HAMMERTON, RW;KRZEMINSKI, KA;NELSON, WJ
通讯作者:
NELSON, WJ