Regulation of plant plasma membrane H+- and Ca2+-ATPases by terminal domains

In the last few years, major progress has been made to elucidate the structure, function, and regulation of P-type plasma membrane H(+)-and Ca(2+)-ATPases. Even though a number of regulatory proteins have been identified, many pieces are still lacking in order to understand the complete regulatory m...

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Bibliographic Details
Published in:	Journal of bioenergetics and biomembranes Vol. 37; no. 6; pp. 369 - 374
Main Authors:	Baekgaard, Lone, Fuglsang, Anja T, Palmgren, Michael G
Format:	Journal Article
Language:	English
Published:	United States Springer Nature B.V 01-12-2005
Subjects:	Calcium Calcium ions Calcium-Transporting ATPases - antagonists & inhibitors Calcium-Transporting ATPases - chemistry Domains Homeostasis Hydrogen Membrane Proteins Membranes Plants - enzymology Plants - metabolism Protein Structure, Tertiary Proteins Proton-Translocating ATPases - antagonists & inhibitors Proton-Translocating ATPases - chemistry Regulation Regulatory mechanisms (biology) Regulatory proteins Structure-function relationships
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Summary:	In the last few years, major progress has been made to elucidate the structure, function, and regulation of P-type plasma membrane H(+)-and Ca(2+)-ATPases. Even though a number of regulatory proteins have been identified, many pieces are still lacking in order to understand the complete regulatory mechanisms of these pumps. In plant plasma membrane H(+)- and Ca(2+)-ATPases, autoinhibitory domains are situated in the C- and N-terminal domains, respectively. A model for a common mechanism of autoinhibition is discussed.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1
ISSN:	0145-479X 1573-6881
DOI:	10.1007/s10863-005-9473-0