Role of A Kinase Anchor Proteins in the Tissue-Specific Regulation of Lipoprotein Lipase

Gouri Ranganathan, Irina Pokrovskaya, Subramanian Ranganathan, Philip A. Kern
2005 Molecular Endocrinology  
Activation of protein kinase A by catecholamines inhibits lipoprotein lipase (LPL) activity through the elaboration of an RNA binding complex, which inhibits LPL translation by binding to the 3-untranslated region of the LPL mRNA. To better define this process, we reconstituted the inhibitory RNA binding complex in vitro and demonstrated that the K homology (KH) domain of A kinase anchor protein (AKAP) 121/149 plays a vital role in the inhibition of LPL translation. Inhibition of LPL
more » ... n of LPL translation occurred in vitro only when the C␣ subunit, R subunit, and AKAP 149 were present. Using different glutathione-S-transferase fusion proteins of AKAP 149, sequences containing the KH domain were required for inhibition of LPL translation, and the inhibition of AKAP 121 expression in 3T3-F442A adipocytes with short interfering RNA resulted in loss of epinephrine-mediated translation inhibition.
doi:10.1210/me.2005-0144 pmid:15961507 fatcat:mllc5m6rvjgl3jbejpoh5yvfge