Phosphoglycerate mutase in mammalian striated muscles: Subcellular localization and binding partners

Abstract 

Contrary to previously published data, we have found that in mammalian skeletal muscles, phosphoglycerate mutase (PGM) is organized in a regular, striated fashion within the sarcomere. In the absence of the enzyme effectors, PGM localizes mainly at the M-line, but under conditions typical for contracting muscle, the enzyme accumulates within the I-band of the sarcomere. Searching for muscle PGM binding partners, we have found that PGM interacts with several enzymes of triose phosphate metabolism. It might suggest that PGM is a central structural element of the muscle glycolytic complex located within the isotropic region of the sarcomere.

Structured summary

MINT-7034028: PGM (uniprotkb:P16290) physically interacts (MI:0218) with lactate dehydrogenase B (uniprotkb:P42123), lactate dehydrogenase A (uniprotkb:P04642), G3PDH (uniprotkb:P04797), aldolase (uniprotkb:P05065), Creatine kinase (uniprotkb:P07335), phPhosphoglycerate kinase (uniprotkb:P16617) and Enolase (uniprotkb:P04764) by pull down (MI:0096)

Abbreviations: BSA, bovine serum albumin, DTT, dithiothreitol, EDTA, ethylenediaminetetraacetic acid, PEG, polyethylene glycol, PK, pyruvate kinase, PMSF, phenylmethylsulfonyl fluoride, TIM, triosephosphate isomerase, TRIS, tris(hydroxymethyl)aminomethane, TRITC, tetramethyl rhodamine isothiocyanate

Keywords: Glycolysis, Interaction, Localization, Muscle, Phosphoglycerate mutase