The INDRA Database: Results
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"Upon phosphorylation of Rb1 by the cyclin-dependent kinases Cdk4 and Cdk6, the E2F transcription factors are released from Rb1 [32] ."
reach
"Therefore, it is conceivable to expect that HTLV-1 infection and Tax expression inactivates both p16ink4 and p15ink4 resulting in activation of Cdk4, which subsequently phosphorylates Rb protein to releases E2F."
sparser
"Cyclin D1 and CDK4 phosphorylate and inactivate Rb during the G1/S transition, thereby allowing cell cycle progression to occur [6] ."
rlimsp
"The data suggest that the redundancy in phosphorylation of RB by CDK2 and CDK4 in Nalm-6 extracts is limited."
sparser
"Rb is phosphorylated by CDK2, CDK4 and CDK6, which are inhibited by p16, p21 and p27 (CKI: cyclin-dependent kinase inhibitor)."
reach
"The first one refers to the extent to which Cdk4 contributes to the pseudo-hyper-phosphorylation of pRb, whereas the second one refers to the metabolic rate of the cell."
reach
"For this purpose, cyclinD1 and Cdk4 phosphorylates only RB, but not FOXM1c, so that cyclinD1 and Cdk4 increases the transcriptional activity of FOXM1c without phosphorylating FOXM1c and activates FOXM1c independently of cyclin and Cdk phosphorylation sites in FOXM1c."
reach
"We conclude that a genetic background deprived of decorin favors cell cycle progression of HCC by repressing AP4, inducing p21 Waf1 and Cip1, and enhancing phosphorylation of P-Rb at Ser780 by CDK4 and CyclinD complex."
sparser
"Phosphorylation of pRb by Cdk4-cyclin D at specific site Ser780 inactivates pRb and leads to release of E2F proteins from the inhibitory pRb-E2F-complex [ xref ]."
rlimsp
"Cdk4 specific phosphorylation of pRb on Ser780 and were normalized to total amount of pRb, β-actin served as internal control."
signor
"Cyclin d1 is known to activate cdk4, which then phosphorylates the rb protein, leading to cell cycle progression."
sparser
"Masatoshi et al. demonstrated that cyclin D-CDK4 complex is able to phosphorylate Rb at S780 in vivo and in vitro [ xref ]."
sparser
"We found that phorbol ester induces unusually early expression of cyclin D2 in B-1 but not B-2 cells, that this early-expressed cyclin D2 associates with Cdk4, and that this correlates with assembly of active kinase complexes and phosphorylation of Rb at the Cdk4 phosphoacceptor Ser 780 site."
reach
"Notably both Cdk2 and Cdk4 kinase complexes phosphorylate, during the G 1 to S transition, pRb protein on Ser 795."
reach
"Sequential phosphorylation of pRb by cyclin dependent kinases including CDK4 regulates S-phase of cells [XREF_BIBR], Cyclin D1 and CDK4 complex phosphorylates pRb at Ser 795 residue to induce DNA synthesis [XREF_BIBR], We directly determined the role of miR-21-regulated cyclin D1 in renal cancer cell proliferation."
signor
"Cyclin d1 is known to activate cdk4, which then phosphorylates the rb protein, leading to cell cycle progression."
sparser
"While Cdk4-cyclin D efficiently and specifically phosphorylates pRb on Ser780 and Ser795, Cdk2-cyclin A/E does not."
rlimsp
"The differential effects of phosphorylation on pRb function coincide with modification of distinct sets of sites. Serine 795 is phosphorylated efficiently by Cdk4, even in the absence of an intact LXCXE motif in cyclin D, but not by Cdk2 or Cdk3."
rlimsp
"Phosphorylation of serines 608/612 inhibits binding of E2F-1 to RB. In Nalm-6 acute lymphoblastic leukemia extracts, serine 608 is phosphorylated by CDK4/6 complexes but not by CDK2. We reasoned that phosphorylation of serines 608/612 by redundant CDKs could accelerate phospho group formation and determined which G1 CDK contributes to serine 612 phosphorylation. Here, we report that CDK4 complexes from Nalm-6 extracts phosphorylated in vitro the CDK2-preferred serine 612, which was inhibited by p16INK4a, and fascaplysin. In contrast, serine 780 and serine 795 were efficiently phosphorylated by CDK4 but not by CDK2."
signor
"We demonstrate that phosphorylation by either cdk2-cyclin a, which phosphorylates t821, or cdk4-cyclin d1, which phosphorylates threonine 826, can disable prb for subsequent binding of an lxcxe protein."
reach
"At the cellular level, the TL mediated decrease in CDK4 protein levels in HeLa cells causes reduced phosphorylation of Rb resulting in cell cycle arrest at the G1 phase."
reach
"Specifically, increased expression of CDK4 due to elevations in copy number and through the activation of the mTOR pathway via PTEN and TSC2 mutations leads to phosphorylation of Rb in a majority of human PanNETs."
reach
"Frankincense essential oil suppressed cyclin D1 and cdk4 expression may lead to suppressed Rb phosphorylation which results in suppressed cell cycle progression in pancreatic cancer cells [XREF_BIBR]."
reach
"Over-expression of cyclin-D or CDK4 kinases from amplification, mutation, or chromosomal translocation can lead to enhanced Rb phosphorylation and poor prognosis."
reach
"RAS and CDK4 co-expression promotes Rb phosphorylation, ultimately resulting in human invasive neoplasm."
reach
"Higher levels of CDK4 may lead to RB phosphorylation impairing its function in cell cycle control [XREF_BIBR]."
reach
"Furthermore, ectopic expression of cyclin D1 but not CDK4, substantially increased RB phosphorylation and conferred substantial resistance to CDK4/6 inhibitors in SCCOHT-1 and BIN-67 cells."
bel
"\"progression through G1 phase of cell cycle requires phosphorylation of the retinoblastoma gene product (pRb) by the cyclin D-dependent serine-threonine kinases CDK4 and CDK6"
bel
"By inhibiting selectively either cdk4/6 or cdk2, we show that endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes. Furthermore, cyclin E-cdk2 is unable to phosphorylate pRb in the absence of prior phosphorylation by cyclin D-cdk4/6 complexes."
bel
"By inhibiting selectively either cdk4/6 or cdk2, we show that endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes. Furthermore, cyclin E-cdk2 is unable to phosphorylate pRb in the absence of prior phosphorylation by cyclin D-cdk4/6 complexes."
signor
"Phosphorylated by cdk6 and cdk4, and subsequently by cdk2 at ser-567 in g1, thereby releasing e2f1 which is then able to activate cell growth. Here we show that although these cdks phosphorylate multiple residues in prb, they do so with different residue selectivities in vitro;thr821 and thr826 are preferentially phosphorylated by cdk6 and cdk4, respectively."
sparser
"This study shows that Ser-608 in pRb was phosphorylated in vitro by Cdk4 and Cdk6."
reach
"CDK4 and CDK6 specific phosphorylation of Rb on serine 807-811 (pSRb) confirmed that the CDK4 and cyclin D1 holoenzyme was active in MCL cells, along with CDK6 and cyclin D1 in MCL7 and CDK4 and cyclin D2 in MCL6."
bel
"The pRb phosphorylated in vitro by Cdk4 was inactive as a growth suppressor upon microinjection, but pRb phosphorylated by Cdk2 or Cdk3 retained cell cycle arrest activity. While these kinases efficiently phosphorylate a common set of residues, including S373 and S788, cyclin D1/Cdk4 was a much more efficient kinase for S795 than the other kinases examined."
bel
"The pRb phosphorylated in vitro by Cdk4 was inactive as a growth suppressor upon microinjection, but pRb phosphorylated by Cdk2 or Cdk3 retained cell cycle arrest activity. While these kinases efficiently phosphorylate a common set of residues, including S373 and S788, cyclin D1/Cdk4 was a much more efficient kinase for S795 than the other kinases examined."
reach
"We found that Costello syndrome fibroblasts display elevated level of Rb phosphorylation on serine 780 (Ser (P)-780-Rb) and that pharmacological inhibition of Ras with radicicol, Mek and Erk with PD98059, or cyclin dependent kinase 4 with PD0332991 not only leads to down-regulation of Ser (P)-780-Rb levels but also enhances Rb phosphorylation on threonine 821 (Thr (P)-821-Rb), which coincides with the recovery of elastin production."
signor
"Phosphorylated by cdk6 and cdk4, and subsequently by cdk2 at ser-567 in g1, thereby releasing e2f1 which is then able to activate cell growth. Here we show that although these cdks phosphorylate multiple residues in prb, they do so with different residue selectivities in vitro;thr821 and thr826 are preferentially phosphorylated by cdk6 and cdk4, respectively."