Pumping with plant P-type ATPases

Citation
Mg. Palmgren et Jf. Harper, Pumping with plant P-type ATPases, J EXP BOT, 50, 1999, pp. 883-893
Citations number
78
Categorie Soggetti
Plant Sciences","Animal & Plant Sciences
Journal title
JOURNAL OF EXPERIMENTAL BOTANY
ISSN journal
00220957 → ACNP
Volume
50
Year of publication
1999
Pages
883 - 893
Database
ISI
SICI code
0022-0957(199906)50:<883:PWPPA>2.0.ZU;2-H
Abstract
In the past 10 years, research on P-type ATPases in plants has advanced fro m its roots in biochemistry to molecular biology, genetics, structure, and back to biochemistry. Since the first cloning of a plant proton pump, plant genes have been identified from all five groups of P-type ATPases. These p umps have been implicated in the transport of multiple ions, including prot ons, calcium, manganese, molybdenum, copper, and phospholipids. To mediate similar cellular functions, plants and animals in some cases utilize entire ly different ion pumps. For example, plants utilize an H+- ATPase instead o f an Na+/K+-ATPase to energize the plasma membrane with an electrochemical gradient. Another distinction between plants and animals is that in some ca ses similar pumps are used in different subcellular locations. For example, while in animals the 'plasma membrane'-type calmodulin-regulated Ca2+-ATPa ses are exclusively found in plasma membrane, several plant homologues have been found in endomembrane locations, such as the ER and tonoplast. Throug h multidisciplinary approaches the next decade should reveal insights into important questions, including: What are the ion specificities of various d ivergent pumps? What are the structural changes mediating ion translocation ? What are the cellular and organismal functions of different pumps? How ar e pumps regulated? and, ultimately, How can we use our knowledge of P-type ATPases for applications in agriculture?