TCTEX1D4, a novel protein phosphatase 1 interactor: connecting the phosphatase to the microtubule network.

摘要: Reversible phosphorylation plays an important role as a mechanism of intracellular control in eukaryotes. PPP1, major eukaryotic Ser/Thr-protein phosphatase, acquires its specificity by interacting with different protein regulators, also known PPP1 proteins (PIPs). In the present work we characterized physiologically relevant PIP testis. Using yeast two-hybrid screen human testis cDNA library, identified novel PPP1CC2 isoform, T-complex expressed 1 domain containing 4 (TCTEX1D4) that has recently been described Tctex1 dynein light chain family member. The overlay assays confirm TCTEX1D4 interacts spliced isoforms PPP1CC. Also, binding occurs N-terminus, where consensus motif (PPP1BM) RVSF is present. distribution suggests involvement distinct functions, such TGFβ signaling at blood–testis barrier and acrosome cap formation. Immunofluorescence ejaculated sperm shows flagellum region head. Moreover, co-localize microtubule organizing center (MTOC) microtubules cell cultures. Importantly, PPP1BM seems to be for complex formation, retention MTOC movement along microtubules. These results open new avenues possible roles this dynein, together PPP1. essence TCTEX1D4/PPP1C appears involved dynamics, motility, reaction regulation barrier.