High impact information on Mak

• These results strongly suggest that the Mak complex may play a role in meiosis during spermatogenesis and that a phosphorylated 210-kDa protein is one of the physiological substrates for this protein kinase [1].
• Furthermore, in a testicular cell culture system with 32Pi, the 210-kDa molecule associated with Mak was phosphorylated in vivo on serine and threonine residues [1].
• Testicular germ cell fractionation revealed that Mak products were most abundant in the fraction of the late pachytene stage and that their levels were dramatically decreased in postmeiotic haploid cells [1].
• In this study, we prepared a series of antibodies against synthetic peptides and fusion products of the mak gene and characterized the subcellular localization, protein kinase activity, and association with other cellular proteins of Mak. Mak products were identified as 66- and 60-kDa proteins that specifically appeared in rat testes after puberty [1].
• Amino acids analysis revealed that the N-terminal catalytic domain is 87% identical to the male-germ cell associated kinase (MAK), a cdc2-related serine/threonine kinase found to promote meiosis during spermatogenesis [2].

Associations of Mak with chemical compounds

• Mak transcripts of 2.6- and 3.4 kb were detected in vitamin A-deficient germ cells, but decreased to undetectable levels shortly after retinol replacement to vitamin A-deficient rats [3].
• Retinol differentially regulates male germ cell-associated kinase (mak) messenger ribonucleic acid expression during spermatogenesis [3].

References