The Enzyme Database

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Accepted name: CRIK-subfamily protein kinase
Reaction: (1) ATP + [protein]-L-serine = ADP + [protein]-O-phospho-L-serine
(2) ATP + [protein]-L-threonine = ADP + [protein]-O-phospho-L-threonine
Other name(s): CRIK; CIT; SGK21; Citron; Citron-K; Sticky/Citron Kinase; Citron Rho-Interacting Kinase
Comments: Requires Mg2+. Peptide array data show a preference for phosphorylation of Thr over Ser and a preference for basic residues in the -5 to -1 positions [1]. CRIK is an animal-specific protein kinase that phosphorylates myosin light chain (cf. EC, myosin-light-chain kinase) and is involved in cytokinesis in both mammals and Drosophila. Human CRIK phosphorylates myosin light chain, MYL9/MRLC1 on T19/S20 [2] and GLI2 on S149 [3]. Drosophila CRIK (sticky) interacts with the kinesins Nebbish and Pavarotti, and human CRIK interacts with their orthologs, KIF14 and KIF23/MKLP1 to promote midbody formation during cytokinesis [4]. In Drosophila, CRIK/Sticky catalytic activity was required for this function. Human CRIK is mostly highly expressed in brain, and mutations that alter splicing or kinase activity lead to microcephaly [5, 6], as do knockouts in mouse and rat, and mutations in its interacting partner, the kinesin KIF14 [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Johnson, J.L., Yaron, T.M., Huntsman, E.M., Kerelsky, A., Song, J., Regev, A., Lin, T.Y., Liberatore, K., Cizin, D.M., Cohen, B.M., Vasan, N., Ma, Y., Krismer, K., Robles, J.T., van de Kooij, B., van Vlimmeren, A.E., Andree-Busch, N., Kaufer, N.F., Dorovkov, M.V., Ryazanov, A.G., Takagi, Y., Kastenhuber, E.R., Goncalves, M.D., Hopkins, B.D., Elemento, O., Taatjes, D.J., Maucuer, A., Yamashita, A., Degterev, A., Uduman, M., Lu, J., Landry, S.D., Zhang, B., Cossentino, I., Linding, R., Blenis, J., Hornbeck, P.V., Turk, B.E., Yaffe, M.B. and Cantley, L.C. An atlas of substrate specificities for the human serine/threonine kinome. Nature 613 (2023) 759–766. [DOI] [PMID: 36631611]
2.  Yamashiro, S., Totsukawa, G., Yamakita, Y., Sasaki, Y., Madaule, P., Ishizaki, T., Narumiya, S. and Matsumura, F. Citron kinase, a Rho-dependent kinase, induces di-phosphorylation of regulatory light chain of myosin II. Mol. Biol. Cell 14 (2003) 1745–1756. [DOI] [PMID: 12802051]
3.  Xing, Z., Lin, A., Li, C., Liang, K., Wang, S., Liu, Y., Park, P.K., Qin, L., Wei, Y., Hawke, D.H., Hung, M.C., Lin, C. and Yang, L. lncRNA directs cooperative epigenetic regulation downstream of chemokine signals. Cell 159 (2014) 1110–1125. [DOI] [PMID: 25416949]
4.  Bassi, Z.I., Audusseau, M., Riparbelli, M.G., Callaini, G. and D'Avino, P.P. Citron kinase controls a molecular network required for midbody formation in cytokinesis. Proc. Natl. Acad. Sci. USA 110 (2013) 9782–9787. [DOI] [PMID: 23716662]
5.  Shaheen, R., Hashem, A., Abdel-Salam, G.M., Al-Fadhli, F., Ewida, N. and Alkuraya, F.S. Mutations in CIT, encoding citron rho-interacting serine/threonine kinase, cause severe primary microcephaly in humans. Hum Genet 135 (2016) 1191–1197. [DOI] [PMID: 27503289]
6.  Li, H., Bielas, S.L., Zaki, M.S., Ismail, S., Farfara, D., Um, K., Rosti, R.O., Scott, E.C., Tu, S., Chi, N.C., Gabriel, S., Erson-Omay, E.Z., Ercan-Sencicek, A.G., Yasuno, K., Caglayan, A.O., Kaymakcalan, H., Ekici, B., Bilguvar, K., Gunel, M. and Gleeson, J.G. Biallelic mutations in citron kinase link mitotic cytokinesis to human primary microcephaly. Am. J. Hum. Genet. 99 (2016) 501–510. [DOI] [PMID: 27453578]
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