High impact information on MAST2

• Binding of MAST205 to microtubules requires interaction with other MAPs, since it does not bind to MAP-free tubulin [1].
• Antibodies affinity purified by using one expression clone recognized a 205-kDa protein, termed MAST205, which colocalizes with the spermatid manchette [1].
• The MAST205 protein complex may function to link the signal transduction pathway with the organization of manchette microtubules [1].
• Sequencing of full-length cDNA clones encoding MAST205 revealed it to be a novel serine/threonine kinase with a catalytic domain related to those of the A and C families [1].
• RNA interference targeting MAST205, a 205-kDa serine/threonine kinase, and transfection of dominant negative MAST205 mutants also mimic this type II macrophage phenotype [2].

Biological context of MAST2

• The objective of this study was to further delineate the role of MAST205 in mammalian spermiogenesis [3].
• The domain required for degradation of MAST205 after Fcgamma receptor activation resides within the N-terminal 261 residues, and degradation is triggered by protein kinase C isoform phosphorylation of Ser/Thr residues [2].

Anatomical context of MAST2

• We recently cloned a novel 205-kDa manchette microtubule-associated serine/threonine protein kinase (MAST205) from mouse testis [3].
• Taken together, these results indicate that the MAST205 complex functions in spermatid maturation in mammals [3].
• While MAST205 RNA levels were similar in pachytene spermatocytes, round spermatids, and residual bodies, MAST205 protein could be detected only in round spermatids and residual bodies [3].
• Multiple heterologous protein species were seen in immunoprecipitates from 35S-labeled mouse seminiferous tubules using an affinity-purified MAST205 antiserum [3].
• Furthermore, MAST205 protein and the associated kinase activity were not detected in epididymal spermatozoa, indicating that MAST205 protein is either excluded from, or degraded in, the latter cell type [3].

References