<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>2(5)</volume><submitter>Korrodi-Gregorio L</submitter><pubmed_abstract>Reversible phosphorylation plays an important role as a mechanism of intracellular control in eukaryotes. PPP1, a major eukaryotic Ser/Thr-protein phosphatase, acquires its specificity by interacting with different protein regulators, also known as PPP1 interacting proteins (PIPs). In the present work we characterized a physiologically relevant PIP in testis. Using a yeast two-hybrid screen with a human testis cDNA library, we identified a novel PIP of PPP1CC2 isoform, the T-complex testis expressed protein 1 domain containing 4 (TCTEX1D4) that has recently been described as a Tctex1 dynein light chain family member. The overlay assays confirm that TCTEX1D4 interacts with the different spliced isoforms of PPP1CC. Also, the binding domain occurs in the N-terminus, where a consensus PPP1 bin</pubmed_abstract><journal>Biology open</journal><pagination>453-65</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3654263</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>TCTEX1D4, a novel protein phosphatase 1 interactor: connecting the phosphatase to the microtubule network.</pubmed_title><pmcid>PMC3654263</pmcid><pubmed_authors>Brauns AK</pubmed_authors><pubmed_authors>Luers G</pubmed_authors><pubmed_authors>Fardilha M</pubmed_authors><pubmed_authors>Esteves SL</pubmed_authors><pubmed_authors>da Cruz E Silva EF</pubmed_authors><pubmed_authors>Esteves PJ</pubmed_authors><pubmed_authors>da Cruz E Silva OA</pubmed_authors><pubmed_authors>Korrodi-Gregorio L</pubmed_authors><pubmed_authors>Freitas MJ</pubmed_authors><pubmed_authors>Vieira SI</pubmed_authors><pubmed_authors>Silva JV</pubmed_authors><pubmed_authors>Abrantes J</pubmed_authors></additional><is_claimable>false</is_claimable><name>TCTEX1D4, a novel protein phosphatase 1 interactor: connecting the phosphatase to the microtubule network.</name><description>Reversible phosphorylation plays an important role as a mechanism of intracellular control in eukaryotes. PPP1, a major eukaryotic Ser/Thr-protein phosphatase, acquires its specificity by interacting with different protein regulators, also known as PPP1 interacting proteins (PIPs). In the present work we characterized a physiologically relevant PIP in testis. Using a yeast two-hybrid screen with a human testis cDNA library, we identified a novel PIP of PPP1CC2 isoform, the T-complex testis expressed protein 1 domain containing 4 (TCTEX1D4) that has recently been described as a Tctex1 dynein light chain family member. The overlay assays confirm that TCTEX1D4 interacts with the different spliced isoforms of PPP1CC. Also, the binding domain occurs in the N-terminus, where a consensus PPP1 bin</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 May</publication><modification>2026-05-03T13:42:00.938Z</modification><creation>2026-04-07T19:14:38.085Z</creation></dates><accession>S-EPMC3654263</accession><cross_references><pubmed>23789093</pubmed><doi>10.1242/bio.20131065</doi></cross_references></HashMap>