Cdc14b regulates mammalian RNA polymerase II and represses cell cycle transcription

Guillamot, María; Manchado, Eusebio; Chiesa, Massimo; Gómez‐López, Gonzalo; Pisano, David G.; Sacristán, María P.; Malumbres, Marcos

doi:10.1038/srep00189

Cited by 38 publications

(47 citation statements)

References 28 publications

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“…This role may be related to that of human Cdc14B, which has also been implicated in the repression of cell cycle transcription (76). Clp1 may regulate Sep1 (mitosis/cytokinesis) and multiple components of the MBF transcription factor complex (50) as well as Mbx1 (55).…”

Section: Fig 5 Clp1 Dephosphorylates the Candidate Substrates (A-h)mentioning

confidence: 99%

Comprehensive Proteomics Analysis Reveals New Substrates and Regulators of the Fission Yeast Clp1/Cdc14 Phosphatase

Chen

Broadus

McLean

et al. 2013

Molecular & Cellular Proteomics

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The conserved family of Cdc14 phosphatases targets cyclin-dependent kinase substrates in yeast, mediating late mitotic signaling events. To discover substrates and regulators of the Schizosaccharomyces pombe Cdc14 phosphatase Clp1, TAP-tagged Clp1, and a substrate trapping mutant (Clp1-C286S) were purified from asynchronous and mitotic (prometaphase and anaphase) cells and binding partners were identified by 2D-LC-MS/MS. Over 100 Clp1-interacting proteins were consistently identified, over 70 of these were enriched in Clp1-C286S-TAP (potential substrates) and we and others detected Cdk1 phosphorylation sites in over half (44/73) of these potential substrates. According to GO annotations, Clp1-interacting proteins are involved in many essential cellular processes including mitosis, cytokinesis, ribosome biogenesis, transcription, and trafficking among others. We confirmed association and dephosphorylation of multiple candidate substrates, including a key scaffolding component of the septation initiation network called Cdc11, an essential kinase of the conserved morphogenesis-related NDR kinase network named Shk1, and multiple Mlu1-binding factor transcriptional regulators. In addition, we identified Sal3, a nuclear ␤-importin, as the sole karyopherin required for Clp1 nucleoplasmic shuttling, a key mode of Cdc14 phosphatase regulation. Finally, a handful of proteins were more abundant in wild type Clp1-TAP

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Section: Fig 5 Clp1 Dephosphorylates the Candidate Substrates (A-h)mentioning

confidence: 99%

Comprehensive Proteomics Analysis Reveals New Substrates and Regulators of the Fission Yeast Clp1/Cdc14 Phosphatase

Chen

Broadus

McLean

et al. 2013

Molecular & Cellular Proteomics

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“…More recently, RPAP2 was identified as the human homologue of the yeast Rtr1 phosphatase and dephosphorylates CTD S5-P in vitro and in vivo (Egloff et al, 2012b). Human CDC14A and CDC14B are the orthologs of the yeast M-phase-specific phosphatase Cdc14 and regulate the expression of cell-cycle-specific genes (Guillamot et al, 2011). CDC14A decreases both S5-P and the S2-P in vitro, whereas CDC14B displays a preference for S5 both in vitro and in vivo (Guillamot et al, 2011).…”

Section: Encoders Readers and Decoders Of The Ctd Code Signaturementioning

confidence: 98%

“…Human CDC14A and CDC14B are the orthologs of the yeast M-phase-specific phosphatase Cdc14 and regulate the expression of cell-cycle-specific genes (Guillamot et al, 2011). CDC14A decreases both S5-P and the S2-P in vitro, whereas CDC14B displays a preference for S5 both in vitro and in vivo (Guillamot et al, 2011). Mammalian cells also contain many SCPs (small CTD phosphatases) that include the FCPH (FCP-homology) domain but lack the BRCT (BRCA1 C-terminal) domain of the FCP1 phosphatase (Yeo et al, 2003).…”

Section: Encoders Readers and Decoders Of The Ctd Code Signaturementioning

confidence: 99%

Modifications of RNA polymerase II CTD: Connections to the histone code and cellular function

Srivastava

Ahn

2015

Biotechnology Advances

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“…RENT is similar to the Scp associated REST complex in that it helps to silence gene expression [170, 171]. Cdc14 is thought to contribute to transcription silencing by dephosphorylating CTD [60, 61]. Recombinant Cdc14 can dephosphorylate purified, hyperphosphorylated CTD substrate in vitro .…”

Section: Introductionmentioning

confidence: 99%

Dephosphorylating eukaryotic RNA polymerase II

Mayfield

Burkholder

Zhang

2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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The phosphorylation state of the C-terminal domain of RNA Polymerase II is required for the temporal and spatial recruitment of various factors that mediate transcription and RNA processing throughout the transcriptional cycle. Therefore, changes in CTD phosphorylation by site-specific kinases/phosphatases are critical for the accurate transmission of information during transcription. Unlike kinases, CTD phosphatases have been traditionally neglected as they are thought to act as passive negative regulators that remove all phosphate marks at the conclusion of transcription. This over-simplified view has been disputed in recent years and new data asserts the active and regulatory role phosphatases play in transcription. We now know that CTD phosphatases ensure the proper transition between different stages of transcription, balance the distribution of phosphorylation for accurate termination and re-initiation, and prevent inappropriate expression of certain genes. In this review, we focus on the specific roles of CTD phosphatases in regulating transcription. In particular, we emphasize how specificity and timing of dephosphorylation is achieved for these phosphatases and consider the various regulatory factors that affect these dynamics.

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Cdc14b regulates mammalian RNA polymerase II and represses cell cycle transcription

Cited by 38 publications

References 28 publications

Comprehensive Proteomics Analysis Reveals New Substrates and Regulators of the Fission Yeast Clp1/Cdc14 Phosphatase

Comprehensive Proteomics Analysis Reveals New Substrates and Regulators of the Fission Yeast Clp1/Cdc14 Phosphatase

Modifications of RNA polymerase II CTD: Connections to the histone code and cellular function

Dephosphorylating eukaryotic RNA polymerase II

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