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First published online August 9, 2006

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ADAMant about location

ADAM family proteins are membrane proteins that were first shown to function in sperm-egg fusion. Each contains a disintegrin domain and a metalloproteinase domain (though not all are catalytically active), and they are important regulators of cell adhesion and recognition - for example, in muscle and brain development. Ulrike Novak and colleagues have been studying how ADAM22, a catalytically inactive ADAM expressed in the brain, reaches the cell surface. On p. 3296, they report that the cytoplasmic domain of ADAM22 interacts with 14-3-3 proteins. These proteins regulate many important cellular processes - usually by binding to phosphorylated residues in their target. The authors show that brain-expressed 14-3-3 proteins interact preferentially with the phosphorylated precursor form of ADAM22, mainly through the first of two 14-3-3-binding sites in its cytoplasmic tail; ADAM22 mutants that lack these binding sites fail to accumulate normally at the cell surface unless an ER-retention motif is also deleted. Thus, 14-3-3 proteins might help to transport ADAM22 to the cell membrane by masking ER-retention signals - a novel role for this family.

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Related articles in JCS:

Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members

Nathan J. Gödde, Giovanna M. D'Abaco, Lucy Paradiso, and Ulrike Novak
JCS 2006 119: 3296-3305. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?