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CDK4 phosphorylates RB1. 10 / 750
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"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."

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"Many studies have shown that the cyclin D1 and CDK4 complex enters the nucleus and phosphorylates RB family proteins during the cell cycle control of proliferating cells."

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"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."

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"Finally, CDK4 and CDK6 may have different preferences for phosphorylation of specific sites in pRb protein [ xref ], and we have recently found distinct specificities of pRb phosphorylation by CDK4 activated by cyclin D1 or cyclin D3 [ xref ]."

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"The CDK4 (or CDK6) catalytic complex acts early in G1 to phosphorylate Rb [XREF_BIBR - XREF_BIBR]."

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"XREF_BIBR In late G 1, a significant hyperphosphorylation of the pRB by CDK4 and CDK6 in complex with D cyclins (D1, D2, D3) occurs."

sparser
"Furthermore, we identified their expression levels of CDK4 and phosphorylated RB1 were reduced in response to miR p-27-5p over-expression."

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"Cyclin D1 can bind to and activate CDK4 and CDK6, which phosphorylates RB protein and promotes the release of E2F and cell cycle progression."

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"For example, gankyrin competes with p16 for binding to CDK4, thus blocking the CDK4-inhibitory activity of p16; p34 SEI1 (SERTAD1) is able to bind to the CDK4-cyclin D1 complex and enhance the latter 's kinase activity; BMI1 (B lymphoma Mo-MLV insertion region 1 homolog, a polycomb ring finger protein) down-regulates the expression of p16 (CDKN2A) and p15 (CDKN2B) genes, which consequently promotes CDK4 mediated phosphorylation of pRb."

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"Cyclin D1 and the CDK4 complex phosphorylate pRB, allowing entry into the cell cycle [27,28,29] ."
CDK4 phosphorylates RB1 on S780. 10 / 30
1 1 4 | 7 15 1

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"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."

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sparser
"Conversely, during cell cycle progression, retinoblastoma protein (pRB) is sequentially phosphorylated by CYCLIN-CDK complexes, and CYCLIN D1-CDK4 specifically phosphorylates pRB on the Ser780 residue, leading to its inactivation and the release of E2F. xref In accordance with our transcriptomic data showing that both CCND1 and CDK4 gene expression were downregulated upon TYRO3 depletion (supplementary table  xref ), we observed lower levels of pRB phosphorylation at Ser780 in the three cell lines studied after TYRO3 knockdown, which may, therefore, lead to pRB activation and E2F inactivation, as suggested by IPA analysis of our transcriptomic data (Fig.  xref , lower panel)."

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"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."

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"The resulting loss of CDK4 function prevented downstream Rb phosphorylation at S780 and S807/811, leading to cell cycle arrest by failure at the S-phase checkpoint."

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"PRb is also phosphorylated at S780 by the cyclin D1 and cdk4 complex but not by the cyclin E and cdk2 complex."

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"It is clear that CDK4 plays a critical role in the G1-S transition of the cell cycle by phosphorylating the retinoblastoma protein (pRb) and Ser-780 residue on Rb is specifically phosphorylated by CDK[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Masatoshi et al. demonstrated that cyclin D and CDK4 complex is able to phosphorylate Rb at S780 in vivo and in vitro [XREF_BIBR]."
CDK4 phosphorylates RB1 on S795. 10 / 12
1 1 2 | 3 3 2

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"Notably both Cdk2 and Cdk4 kinase complexes phosphorylate, during the G 1 to S transition, pRb protein on Ser 795."

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"Furthermore, there is no direct evidence indicating that the suppression of cdk4 protein induced by TGF-beta1 leads to inhibition of pRb phosphorylation at Ser795, although pRb reportedly is phosphory[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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."

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"Furthermore, there is no direct evidence indicating that the suppression of cdk4 protein induced by TGF-β1 leads to inhibition of pRb phosphorylation at Ser795, although pRb reportedly is phosphorylat[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"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."

"Cyclin d1 is known to activate cdk4, which then phosphorylates the rb protein, leading to cell cycle progression."

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."
CDK4 phosphorylates RB1 on T826. 9 / 9
1 1 7 |

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"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."

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Modified CDK4 leads to the phosphorylation of RB1. 9 / 9
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"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."

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"CDK2 and CDK4 overexpression in oral SCC may elevate pRB phosphorylation and permit more rapid entry of cancer cells into S-phase."

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"PGA 2 was shown to elevate p21 expression and inhibit the activation of cdk2 and cdk4 due to dramatic decrease in the levels of cyclinD1 and cdk4, blocking the hyperphosphorylation of retinoblastoma p[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Higher levels of CDK4 may lead to RB phosphorylation impairing its function in cell cycle control [XREF_BIBR]."

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"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]."

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"Over-expression of cyclin-D or CDK4 kinases from amplification, mutation, or chromosomal translocation can lead to enhanced Rb phosphorylation and poor prognosis."

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"RAS and CDK4 co-expression promotes Rb phosphorylation, ultimately resulting in human invasive neoplasm."

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"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."

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"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."
CDK4 phosphorylates RB1 on S811. 7 / 7
1 1 1 | 4

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"The resulting loss of CDK4 function prevented downstream Rb phosphorylation at S780 and S807/811, leading to cell cycle arrest by failure at the S-phase checkpoint."

"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."

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"Retinoblastoma protein (pRb) phosphorylation on Ser807 and Ser811 (p-pRb) by CDK4 and CDK6 and D-type cyclins, represents the first step of cell cycle progression after cell activation."

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"CDK4 phosphorylates S807/S811 on Rb, and this partial phosphorylation is needed for CDK2 phosphorylation ."

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"Phosphorylation of Rb at serine 807/811 is mediated primarily by cyclinD and CDK4 (Knudson and Wang, 1996)."
CDK4 phosphorylates RB1 on S807. 6 / 6
1 1 | 4

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"CDK4 phosphorylates S807/S811 on Rb, and this partial phosphorylation is needed for CDK2 phosphorylation ."

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"Phosphorylation of Rb at serine 807/811 is mediated primarily by cyclinD and CDK4 (Knudson and Wang, 1996)."

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"Retinoblastoma protein (pRb) phosphorylation on Ser807 and Ser811 (p-pRb) by CDK4 and CDK6 and D-type cyclins, represents the first step of cell cycle progression after cell activation."

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"The resulting loss of CDK4 function prevented downstream Rb phosphorylation at S780 and S807/811, leading to cell cycle arrest by failure at the S-phase checkpoint."
Kinase-active CDK4 phosphorylates RB1 on serine. 4 / 4
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"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."

"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."

"\"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"

"\"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"
CDK4 phosphorylates RB1 on S788. 4 / 4
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CDK4 phosphorylates RB1 on T356. 3 / 3
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CDK4 phosphorylates RB1 on S608. 3 / 3
1 | 1 1

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"This study shows that Ser-608 in pRb was phosphorylated in vitro by Cdk4 and Cdk6."

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"We then directly examined Rb phosphorylation in MECs of different genotypes by using an antibody specifically recognizing Rb proteins phosphorylated at Ser608 by CDK4 and CDK6 [XREF_BIBR, XREF_BIBR], the functional targets of p16."
CDK4 phosphorylates RB1 on serine. 2 / 2
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"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."

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"PD 0332991 completely inhibited CDK4 and CDK6 within 24 hours, as indicated by the loss of CDK4 and CDK6 specific phosphorylation of Rb on serine 807-811 (pRb), arrested the cell cycle in G1, and marked reduction of DNA replication as measured by BrdU pulse labeling (XREF_FIG)."
CDK4 leads to the phosphorylation of RB1 on T821. 1 / 1
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"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."
CDK4 phosphorylates RB1 on T252. 1 / 1
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CDK4 phosphorylates RB1 on S249. 1 / 1
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"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."
CDK4 phosphorylates RB1 on T5. 1 / 1
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Kinase-active CDK4 leads to the phosphorylation of RB1 on S795. 1 / 1
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"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."
Mutated CDK4 leads to the phosphorylation of RB1. 1 / 1
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"Thus, the mutant CDK4 Cyclin D complex induces phosphorylation of RB protein in the host cell, based on the high homology among multiple species."
CDK4 phosphorylates phosphorylated RB1. 1 / 1
| 1

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"Hyperphosphorylation of pRb by cyclin D1 and cdk4 complex releases E2F, a necessary event for the G1 to S transition, and causes a suspension of G1 arrest.The antibody to pRb (clone G3-245) used in th[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
CDK4-R24C leads to the phosphorylation of RB1. 1 / 1
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"Exogenous expression of an R24C mutant of CDK4, which cannot be bound by the p16INK4A protein and cyclin D1 therefore induces constitutive activation of the cyclin D-CDK4 complex, and induces pRB phosphorylation, resulting in escape from premature senescence."
CDK4 phosphorylates RB1 on S612. 1 / 1
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CDK4 phosphorylates RB1 on T373. 1 / 1
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CDK4 phosphorylates RB1 on threonine. 1 / 1
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"More specifically, CDK4 encodes a cyclindependent serine-threonine kinase in response to mitogenic or proliferation-promoting stimuli and interacts with cyclin D1 to phosphorylate the tumor suppressor protein Rb (109, 110) ."
Kinase-active CDK4 leads to the phosphorylation of RB1 on S788. 1 / 1
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"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."