How Long to Read Regulation of the Ampk Signaling Pathway Activation Via Mitochondrial Adenylate Kinase Isoenzyme 4

By Jocelyn Diane Rodriguez

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Description

Adenylate Kinases are phosphotransferase enzymes that catalyze the interconversion of adenosine nucleotides in the mitochondria. Human adenylate kinase 4 (AK4), is unique in its role in cellular bioenergetics, homeostasis, and modulation of Adenosine 5'monophosphate activated protein kinase (AMPK) pathways. AMPK signaling is a key element in the regulation of many biological processes such as cell survival, autophagy and mitochondrial biogenesis. Strikingly, AMPK has been linked to tumorigenesis and cancer cell progression. Similarly, AK4 has been linked to cancer promotion, with studies demonstrating that AK4 knockdown in vivo mice models produce smaller tumors. While biological effects of AMPK and AK4 have been demonstrated, the mechanism by which these proteins are associated or if AK4 activates the AMPK pathway remains unclear. A known mode of AMPK activation is through upstream kinases: Serine-Threonine Liver Kinase Îø-1 (LKB1) and Calmodulin Kinase Kinase Îø (CAMKKÎø) phosphorylating AMPK's active site at residue Thr172. The mechanism for upstream kinases activating AMPK however, remains unknown. I hypothesize that AK4 is a missing link in the activation pathway of AMPK.

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