The encoded cytosolic protein and mitochondrial glycerol-3-phosphate dehydrogenase also form a glycerol phosphate shuttle that facilitates the transfer of reducing equivalents from the cytosol to mitochondria.
Mutations in this gene are a cause of transient infantile hypertriglyceridemia. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
Gudayol M, Vidal J, Usac EF, Morales A, Fabregat ME, Fernández-Checa JC, Novials A, Gomis R (2001). "Identification and functional analysis of mutations in FAD-binding domain of mitochondrial glycerophosphate dehydrogenase in caucasian patients with type 2 diabetes mellitus". Endocrine. 16 (1): 39–42. doi:10.1385/ENDO:16:1:39. PMID11822825. S2CID30120853.
Swierczynski J, Zabrocka L, Goyke E, Raczynska S, Adamonis W, Sledzinski Z (2003). "Enhanced glycerol 3-phosphate dehydrogenase activity in adipose tissue of obese humans". Mol. Cell. Biochem. 254 (1–2): 55–9. doi:10.1023/a:1027332523114. PMID14674682. S2CID25108711.
Ou X, Ji C, Han X, Zhao X, Li X, Mao Y, Wong LL, Bartlam M, Rao Z (2006). "Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1)". J. Mol. Biol. 357 (3): 858–69. doi:10.1016/j.jmb.2005.12.074. PMID16460752.
Park JJ, Berggren JR, Hulver MW, Houmard JA, Hoffman EP (2006). "GRB14, GPD1, and GDF8 as potential network collaborators in weight loss-induced improvements in insulin action in human skeletal muscle". Physiol. Genomics. 27 (2): 114–21. doi:10.1152/physiolgenomics.00045.2006. PMID16849634.