QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online August 20, 2008

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?

...but PAT breaks it down

The proteins of the PAT family are major constituents of cytoplasmic lipid droplets (CLDs), and are thought to have roles in CLD formation and stability. PAT proteins [which include adipophilin (ADPH) and TIP47, among others] have a high degree of amino acid sequence homology in their N-terminal domain (the PAT domain), but little is known about the biological functions of this region. To address this issue, James McManaman and colleagues (p. 2921) now use a deletion mutant of ADPH ( 2,3 ADPH), which lacks amino acids 1-89, to investigate the role of the ADPH PAT domain. The authors show that, in HEK293 cells, full-length ADPH (which is known to depend on triglyceride synthesis for its stability) is degraded unless oleic acid is present; by contrast, 2,3 ADPH and GFP-tagged ADPH are both stable in the absence of oleic acid. When the proteasomal inhibitor MG132 is added, levels of full-length ADPH increase markedly, but the increase in 2,3 ADPH levels is modest. In addition, ADPH (but not 2,3 ADPH) prevents the localisation of TIP47 to CLDs. Notably, when the N-terminal domain of TIP47 is replaced with that of ADPH, the chimeric protein is degraded under the same conditions as ADPH. Thus, the N-terminal PAT domain of ADPH mediates its proteasomal degradation and has additional cellular functions.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

Related articles in JCS:

Multiple functions encoded by the N-terminal PAT domain of adipophilin

David J. Orlicky, Greg DeGala, Carrie Greenwood, Elise S. Bales, Tanya D. Russell, and James L. McManaman
JCS 2008 121: 2921-2929. [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?