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J. Biol. Chem., Vol. 276, Issue 32, 29611, August 10, 2001

This Article Full Text (PDF) All Versions of this Article: 276/32/29611    most recent R100028200v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lingrel, J. B Search for Related Content PubMed PubMed Citation Articles by Lingrel, J. B Social Bookmarking                      What's this?

MINIREVIEW PROLOGUE
Transport ATPase Trafficking Minireview Series^*

From the Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0524

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The P₂-type ATPase family of transport proteins moves ions such as Na⁺, K⁺, H⁺, and Ca²⁺ across cellular membranes against their concentration gradient utilizing ATP as the energy source. The members of this family of P-type ATPases include the Na⁺,K⁺-ATPase, H⁺,K⁺-ATPase, and Ca²⁺-ATPases of higher organisms and the H⁺-ATPase of lower eukaryotes. The gradient produced by these enzymes drives a variety of transport and other biological processes. Major progress during the past few years has identified many structural features of these ATPases, including their membrane topology and cation- and ATP-binding sites; this past year the three-dimensional structure of the Ca²⁺-ATPase was published. These collective studies have provided considerable insight into how this enzyme functions, but many details are yet to be determined, particularly with respect to the structure of the different conformation states occurring during the catalytic cycle.

Other very important features of these enzymes as well as other membrane proteins are their biogenesis, insertion into the appropriate membrane surface, and their regulation via internalization. In the two minireviews of this series, the first one from Carolyn Slayman and her collaborators (The yeast Pma1 proton pump: a model for understanding the biogenesis of plasma membrane proteins by Thierry Ferreira, A. Brett Mason, and Carolyn W. Slayman) describes the biogenesis of the yeast H⁺-ATPase and reviews progress in understanding the trafficking of this plasma membrane protein. Yeast, because of their powerful genetics, is allowing the pathway to be analyzed in considerable detail, and this system also has the advantage of identifying many of the critical proteins in the trafficking process. This minireview also describes checkpoints in the system for handling non-native proteins, particularly those carrying mutations that affect the biogenesis process.

The second minireview from the Caplan laboratory (Ion pumps in polarized cells: sorting and regulation of the Na⁺,K⁺- and H⁺,K⁺-ATPases by Lisa A. Dunbar and Michael J. Caplan) describes the sorting and regulation of the Na⁺,K⁺-ATPase and H⁺,K⁺-ATPase. The major emphasis is on how these enzymes are inserted into either the basolateral or apical surface of polarized cells. Another interesting feature of these enzymes is their internalization, which is also reviewed. The movement between the plasma membrane and internal stores is particularly critical for the function of gastric H⁺,K⁺-ATPase but is also utilized in the case of the Na⁺,K⁺-ATPase and appears to be a common feature in the physiological regulation of this enzyme.

This minireview series provides complementary information using different biological systems to provide extensive insight into the sorting, trafficking, and regulation of the P₂ class of transport ATPases.

	FOOTNOTES

^* This minireview will be reprinted in the 2001 Minireview Compendium, which will be available in December, 2001.

Published, JBC Papers in Press, June 12, 2001, DOI 10.1074/jbc.R100028200

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This Article Full Text (PDF) All Versions of this Article: 276/32/29611    most recent R100028200v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lingrel, J. B Search for Related Content PubMed PubMed Citation Articles by Lingrel, J. B Social Bookmarking                      What's this?