Cyclin K: Difference between revisions
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'''Cyclin-K''' is a [[protein]] that in humans is encoded by the ''CCNK'' [[gene]].<ref name=" | '''Cyclin-K''' is a [[protein]] that in humans is encoded by the ''CCNK'' [[gene]].<ref name="Edwards_1998" /><ref name="Fu_1999">{{cite journal | vauthors = Fu TJ, Peng J, Lee G, Price DH, Flores O | title = Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription | journal = The Journal of Biological Chemistry | volume = 274 | issue = 49 | pages = 34527–30 | date = December 1999 | pmid = 10574912 | pmc = | doi = 10.1074/jbc.274.49.34527 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CCNK cyclin K| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8812| access-date = }}</ref> | ||
== Function == | == Function == | ||
The protein encoded by this gene is a member of the transcription cyclin family. These cyclins may regulate transcription through their association with and activation of cyclin-dependent kinases ( | The protein encoded by this gene is a member of the transcription cyclin family. These cyclins may regulate [[Transcription (biology)|transcription]] through their association with and activation of [[Cyclin-dependent kinase|cyclin-dependent kinases]] (CDKs) through conformational changes.<ref name="Baek_2007">{{cite journal | vauthors = Baek K, Brown RS, Birrane G, Ladias JA | title = Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9 | journal = Journal of Molecular Biology | volume = 366 | issue = 2 | pages = 563–73 | date = February 2007 | pmid = 17169370 | pmc = 1852425 | doi = 10.1016/j.jmb.2006.11.057 }}</ref><ref name="Greifenberg_2016">{{cite journal | vauthors = Greifenberg AK, Hönig D, Pilarova K, Düster R, Bartholomeeusen K, Bösken CA, Anand K, Blazek D, Geyer M | title = Structural and Functional Analysis of the Cdk13/Cyclin K Complex | journal = Cell Reports | volume = 14 | issue = 2 | pages = 320–31 | date = January 2016 | pmid = 26748711 | doi = 10.1016/j.celrep.2015.12.025 }}</ref> Activation of CDKs through their cyclin partner, creates kinase complexes that will activate target proteins through [[phosphorylation]]. Targeted proteins can then ultimately regulate decisions of a cell’s progression within the [[cell cycle]] to occur. This gene product may be seen to play a dual role in both regulating CDK and [[RNA polymerase II]] (RNAP2) activities.<ref name="entrez" /> Cyclin K only uses RNA recruitment to activate transcription.<ref name="Kohoutek_2012">{{cite journal | vauthors = Kohoutek J, Blazek D | title = Cyclin K goes with Cdk12 and Cdk13 | journal = Cell Division | volume = 7 | pages = 12 | date = April 2012 | pmid = 22512864 | pmc = 3348076 | doi = 10.1186/1747-1028-7-12 }}</ref> | ||
== Interactions == | == Interactions == | ||
Cyclin K has been shown to [[ | Cyclin K has been shown to interact with multiple CDKs including [[Cyclin-dependent kinase 9|CDK9]] and latest CDK12 and CDK13.<ref name="Fu_1999" /><ref name="Greifenberg_2016" /> Roles include helping to phosphorylate C-terminal domains of subunits of RNAP2.<ref>{{cite journal | vauthors = Edwards MC, Wong C, Elledge SJ | title = Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity | journal = Molecular and Cellular Biology | volume = 18 | issue = 7 | pages = 4291–300 | date = July 1998 | pmid = 9632813 | pmc = 109013 }}</ref> Cyclin K is most noted for its associated induction of processive elongation.<ref name="Baek_2007" /> Also, identified with [[G1 phase|G1]] and [[S phase|S]] phase cyclin activity, however functions are not deeply understood.<ref name="Edwards_1998">{{cite journal | vauthors = Edwards MC, Wong C, Elledge SJ | title = Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity | journal = Molecular and Cellular Biology | volume = 18 | issue = 7 | pages = 4291–300 | date = July 1998 | pmid = 9632813 | pmc = 109013 | doi = }}</ref><ref name="Berro_2008" /> | ||
Cyclin K also interacts with HIV nef protein.<ref>{{cite journal | vauthors = Khan SZ, Mitra D | title = Cyclin K inhibits HIV-1 gene expression and replication by interfering with cyclin-dependent kinase 9 (CDK9)-cyclin T1 interaction in Nef-dependent manner | journal = The Journal of Biological Chemistry | volume = 286 | issue = 26 | pages = | |||
Cyclin K also interacts with HIV nef protein.<ref name="Khan_2011">{{cite journal | vauthors = Khan SZ, Mitra D | title = Cyclin K inhibits HIV-1 gene expression and replication by interfering with cyclin-dependent kinase 9 (CDK9)-cyclin T1 interaction in Nef-dependent manner | journal = The Journal of Biological Chemistry | volume = 286 | issue = 26 | pages = 22943–54 | date = July 2011 | pmid = 21555514 | pmc = 3123062 | doi = 10.1074/jbc.M110.201194 }}</ref> In the presence of overexpressed Nef protein, Cyclin k and CDK9 binding is induced, inhibiting the positive elongation factor of other CDK9 binding complexes, resulting in an inhibition of specific HIV-1 gene expression.<ref name="Greifenberg_2016" /><ref name="Khan_2011" /> CDK 13 may also be characterized to interact with HIV mRNA splicing, alongside Nef, and the underexpression of Gag and Env related proteins. <ref name="Berro_2008">{{cite journal | vauthors = Berro R, Pedati C, Kehn-Hall K, Wu W, Klase Z, Even Y, Genevière AM, Ammosova T, Nekhai S, Kashanchi F | title = CDK13, a new potential human immunodeficiency virus type 1 inhibitory factor regulating viral mRNA splicing | journal = Journal of Virology | volume = 82 | issue = 14 | pages = 7155–66 | date = July 2008 | pmid = 18480452 | doi = 10.1128/JVI.02543-07 | pmc = 2446983 }}</ref><ref name="Kohoutek_2012" /> | |||
Cyclin K is indispensable for Leukemia growth. SETD1A, is also known to bind Cyclin K through its FLOS domain.<ref name="Hoshii_2018">{{cite journal | vauthors = Hoshii T, Cifani P, Feng Z, Huang CH, Koche R, Chen CW, Delaney CD, Lowe SW, Kentsis A, Armstrong SA | title = A Non-catalytic Function of SETD1A Regulates Cyclin K and the DNA Damage Response | journal = Cell | volume = 172 | issue = 5 | pages = 1007–1021.e17 | date = February 2018 | pmid = 29474905 | doi = 10.1016/j.cell.2018.01.032 }}</ref> The interaction is shown to be important to DNA damage response genes and for Leukemia proliferation.<ref name="Kohoutek_2012" /><ref name="Hoshii_2018" /> | |||
== References == | == References == | ||
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{{refbegin | 2}} | {{refbegin | 2}} | ||
* {{cite journal | vauthors = Lin X, Taube R, Fujinaga K, Peterlin BM | title = P-TEFb containing cyclin K and Cdk9 can activate transcription via RNA | journal = The Journal of Biological Chemistry | volume = 277 | issue = 19 | pages = 16873–8 | date = May 2002 | pmid = 11884399 | doi = 10.1074/jbc.M200117200 }} | * {{cite journal | vauthors = Lin X, Taube R, Fujinaga K, Peterlin BM | title = P-TEFb containing cyclin K and Cdk9 can activate transcription via RNA | journal = The Journal of Biological Chemistry | volume = 277 | issue = 19 | pages = 16873–8 | date = May 2002 | pmid = 11884399 | doi = 10.1074/jbc.M200117200 }} | ||
* {{cite journal | vauthors = Mori T, Anazawa Y, Matsui K, Fukuda S, Nakamura Y, Arakawa H | title = Cyclin K as a direct transcriptional target of the p53 tumor suppressor | journal = Neoplasia | volume = 4 | issue = 3 | pages = 268–74 | year = 2002 | pmid = 11988847 | pmc = 1531701 | doi = 10.1038/sj | * {{cite journal | vauthors = Mori T, Anazawa Y, Matsui K, Fukuda S, Nakamura Y, Arakawa H | title = Cyclin K as a direct transcriptional target of the p53 tumor suppressor | journal = Neoplasia | volume = 4 | issue = 3 | pages = 268–74 | year = 2002 | pmid = 11988847 | pmc = 1531701 | doi = 10.1038/sj.neo.7900235 }} | ||
* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = | * {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = August 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }} | ||
* {{cite journal | vauthors = Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY | title = A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration | journal = Cell | volume = 125 | issue = 4 | pages = 801–14 | date = May 2006 | pmid = 16713569 | doi = 10.1016/j.cell.2006.03.032 }} | * {{cite journal | vauthors = Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY | title = A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration | journal = Cell | volume = 125 | issue = 4 | pages = 801–14 | date = May 2006 | pmid = 16713569 | doi = 10.1016/j.cell.2006.03.032 }} | ||
* {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = | * {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = November 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 }} | ||
* {{cite journal | vauthors = Baek K, Brown RS, Birrane G, Ladias JA | title = Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9 | journal = Journal of Molecular Biology | volume = 366 | issue = 2 | pages = 563–73 | date = | * {{cite journal | vauthors = Baek K, Brown RS, Birrane G, Ladias JA | title = Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9 | journal = Journal of Molecular Biology | volume = 366 | issue = 2 | pages = 563–73 | date = February 2007 | pmid = 17169370 | pmc = 1852425 | doi = 10.1016/j.jmb.2006.11.057 }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=8812}} | {{PDB Gallery|geneid=8812}} | ||
{{gene-14-stub}} | {{gene-14-stub}} | ||
Revision as of 22:15, 22 May 2018
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Cyclin-K is a protein that in humans is encoded by the CCNK gene.[1][2][3]
Function
The protein encoded by this gene is a member of the transcription cyclin family. These cyclins may regulate transcription through their association with and activation of cyclin-dependent kinases (CDKs) through conformational changes.[4][5] Activation of CDKs through their cyclin partner, creates kinase complexes that will activate target proteins through phosphorylation. Targeted proteins can then ultimately regulate decisions of a cell’s progression within the cell cycle to occur. This gene product may be seen to play a dual role in both regulating CDK and RNA polymerase II (RNAP2) activities.[3] Cyclin K only uses RNA recruitment to activate transcription.[6]
Interactions
Cyclin K has been shown to interact with multiple CDKs including CDK9 and latest CDK12 and CDK13.[2][5] Roles include helping to phosphorylate C-terminal domains of subunits of RNAP2.[7] Cyclin K is most noted for its associated induction of processive elongation.[4] Also, identified with G1 and S phase cyclin activity, however functions are not deeply understood.[1][8]
Cyclin K also interacts with HIV nef protein.[9] In the presence of overexpressed Nef protein, Cyclin k and CDK9 binding is induced, inhibiting the positive elongation factor of other CDK9 binding complexes, resulting in an inhibition of specific HIV-1 gene expression.[5][9] CDK 13 may also be characterized to interact with HIV mRNA splicing, alongside Nef, and the underexpression of Gag and Env related proteins. [8][6]
Cyclin K is indispensable for Leukemia growth. SETD1A, is also known to bind Cyclin K through its FLOS domain.[10] The interaction is shown to be important to DNA damage response genes and for Leukemia proliferation.[6][10]
References
- ↑ 1.0 1.1 Edwards MC, Wong C, Elledge SJ (July 1998). "Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity". Molecular and Cellular Biology. 18 (7): 4291–300. PMC 109013. PMID 9632813.
- ↑ 2.0 2.1 Fu TJ, Peng J, Lee G, Price DH, Flores O (December 1999). "Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription". The Journal of Biological Chemistry. 274 (49): 34527–30. doi:10.1074/jbc.274.49.34527. PMID 10574912.
- ↑ 3.0 3.1 "Entrez Gene: CCNK cyclin K".
- ↑ 4.0 4.1 Baek K, Brown RS, Birrane G, Ladias JA (February 2007). "Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9". Journal of Molecular Biology. 366 (2): 563–73. doi:10.1016/j.jmb.2006.11.057. PMC 1852425. PMID 17169370.
- ↑ 5.0 5.1 5.2 Greifenberg AK, Hönig D, Pilarova K, Düster R, Bartholomeeusen K, Bösken CA, Anand K, Blazek D, Geyer M (January 2016). "Structural and Functional Analysis of the Cdk13/Cyclin K Complex". Cell Reports. 14 (2): 320–31. doi:10.1016/j.celrep.2015.12.025. PMID 26748711.
- ↑ 6.0 6.1 6.2 Kohoutek J, Blazek D (April 2012). "Cyclin K goes with Cdk12 and Cdk13". Cell Division. 7: 12. doi:10.1186/1747-1028-7-12. PMC 3348076. PMID 22512864.
- ↑ Edwards MC, Wong C, Elledge SJ (July 1998). "Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity". Molecular and Cellular Biology. 18 (7): 4291–300. PMC 109013. PMID 9632813.
- ↑ 8.0 8.1 Berro R, Pedati C, Kehn-Hall K, Wu W, Klase Z, Even Y, Genevière AM, Ammosova T, Nekhai S, Kashanchi F (July 2008). "CDK13, a new potential human immunodeficiency virus type 1 inhibitory factor regulating viral mRNA splicing". Journal of Virology. 82 (14): 7155–66. doi:10.1128/JVI.02543-07. PMC 2446983. PMID 18480452.
- ↑ 9.0 9.1 Khan SZ, Mitra D (July 2011). "Cyclin K inhibits HIV-1 gene expression and replication by interfering with cyclin-dependent kinase 9 (CDK9)-cyclin T1 interaction in Nef-dependent manner". The Journal of Biological Chemistry. 286 (26): 22943–54. doi:10.1074/jbc.M110.201194. PMC 3123062. PMID 21555514.
- ↑ 10.0 10.1 Hoshii T, Cifani P, Feng Z, Huang CH, Koche R, Chen CW, Delaney CD, Lowe SW, Kentsis A, Armstrong SA (February 2018). "A Non-catalytic Function of SETD1A Regulates Cyclin K and the DNA Damage Response". Cell. 172 (5): 1007–1021.e17. doi:10.1016/j.cell.2018.01.032. PMID 29474905.
Further reading
- Lin X, Taube R, Fujinaga K, Peterlin BM (May 2002). "P-TEFb containing cyclin K and Cdk9 can activate transcription via RNA". The Journal of Biological Chemistry. 277 (19): 16873–8. doi:10.1074/jbc.M200117200. PMID 11884399.
- Mori T, Anazawa Y, Matsui K, Fukuda S, Nakamura Y, Arakawa H (2002). "Cyclin K as a direct transcriptional target of the p53 tumor suppressor". Neoplasia. 4 (3): 268–74. doi:10.1038/sj.neo.7900235. PMC 1531701. PMID 11988847.
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
- Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Baek K, Brown RS, Birrane G, Ladias JA (February 2007). "Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9". Journal of Molecular Biology. 366 (2): 563–73. doi:10.1016/j.jmb.2006.11.057. PMC 1852425. PMID 17169370.
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