2004
DOI: 10.1002/dvdy.20146
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PP1β9C interacts with trithorax in Drosophila wing development

Abstract: Type 1 Ser/Thr protein phosphatase (PP1) has many roles in Drosophila: regulating diverse processes from chromatin condensation to transforming growth factor-␤ signaling. The presence of four PP1 genes, PP1␣87B, PP1␤9C, PP1␣96A, and PP1␣13C, encoding very similar proteins complicates analysis of their particular functions. Here, we report that the minor PP1 isoform PP1␤9C binds in vitro and in vivo and genetically interacts with Trithorax (TRX), the archetypal member of the Trx-G family of epigenetic regulator… Show more

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Cited by 6 publications
(7 citation statements)
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“…We previously reported that ectopic HA-tagged PP187B, the major PP1 isoform in Drosophila [43], localised to many discrete chromosomal loci [17], [18]. Like the ectopic protein, we found a large number of discrete sites widely dispersed along the chromosomes that were stained with an anti-peptide antibody to Drosophila PP1 (Figure 5D).…”
Section: Resultsmentioning
confidence: 50%
See 1 more Smart Citation
“…We previously reported that ectopic HA-tagged PP187B, the major PP1 isoform in Drosophila [43], localised to many discrete chromosomal loci [17], [18]. Like the ectopic protein, we found a large number of discrete sites widely dispersed along the chromosomes that were stained with an anti-peptide antibody to Drosophila PP1 (Figure 5D).…”
Section: Resultsmentioning
confidence: 50%
“…In Drosophila , PP1 is found at multiple sites on chromosomes where it has been postulated to play important roles in regulating developmentally controlled gene expression [17], [18]. However, analysing the role of PP1 in transcriptional regulation has been complicated by its pleiotropic roles [19] and broad in vitro substrate specificity.…”
Section: Introductionmentioning
confidence: 99%
“…PP1c binds directly to Trx protein, co-localizes with Trx on polytene chromosomes ( Figure 1) and antagonizes trx function in vivo [5]. Genetic analysis with different isoforms of PP1c indicates that there may be specific roles for different PP1c-Trx complexes [7]. In mammals, PP1c is also a member of a trimeric complex containing PP1c, Gadd34 and SNF5, a component of the SWI/ SNF chromatin-remodelling complex that repositions nucleosomes [8,9].…”
Section: Chromosome-associated Pp1 Complexesmentioning
confidence: 98%
“…An intriguing possibility is that holoenzymes containing the same binding subunit but different PP1c isoforms may have different functions. 24 Ultimately, it will be necessary to verify not only in vivo binding but also to examine functional interactions with different PP1c isoforms in flies. Quantitative assays, such as surface plasmon resonance studies, may also help to resolve whether there are subtle differences in binding affinity that cannot be detected in either the two-hybrid system or by co-immunoprecipitation from fly extracts.…”
Section: Towards a Comprehensive Description Of The Pp1c-interactome mentioning
confidence: 99%
“…Among the proteins that have been identified are homologues of known PP1 regulatory proteins Inhibitor-t, Inhibitor-2 and NIPP1, which have been shown to inhibit PP1c in vitro and/or in vivo [15][16][17][18][19] and the non-muscle myosin targeting subunits MBS and MYPT-75D. 11,20,21 A number of other putative regulatory subunits, have also been identified, including Nebbish/KLP38B, 22 Trithorax, 23,24 Bifocal 25,26 and Sara. 27 Studies on these proteins have implicated PP1 in cellular and developmental processes including: cell division, epigenetic programming, cytoskeleton dynamics, and intracellular signalling pathways involved in pattern formation.…”
Section: Introductionmentioning
confidence: 99%