References
- Hepler PK. Calcium: a central regulator of plant growth and development. Plant Cell. 2005;17:1–4. doi:https://doi.org/10.1105/tpc.105.032508.
- Zuo R, Hu R, Chai G, Xu M, Qi G, Kong Y, Zhou G. Genome-wide identification, classification, and expression analysis of CDPK and its closely related gene families in poplar (Populus trichocarpa). Mol Biol Rep. 2013;40:2645–2662. doi:https://doi.org/10.1007/s11033-012-2351-z.
- Cai H, Cheng J, Yan Y, Xiao Z, Li J, Mou S, Qiu A, Lai Y, Guan D, He S. Genome-wide identification and expression analysis of calcium-dependent protein kinase and its closely related kinase genes in Capsicum annuum. Front Plant Sci. 2015;6:737. doi:https://doi.org/10.3389/fpls.2015.00737.
- Wang JP, Xu YP, Munyampundu JP, Liu TY, Cai XZ. Calcium-dependent protein kinase (CDPK) and CDPK-related kinase (CRK) gene families in tomato: genome-wide identification and functional analyses in disease resistance. Mol Genet Genomics. 2016;291:661–676. doi:https://doi.org/10.1007/s00438-015-1137-0.
- Zhang H, Wei C, Yang X, Chen H, Yang Y, Mo Y, Li H, Zhang Y, Ma J, Yang J, et al. Genome-wide identification and expression analysis of calcium-dependent protein kinase and its related kinase gene families in melon (Cucumis melo L.). PloS One. 2017;12:e0176352. doi:https://doi.org/10.1371/journal.pone.0176352.
- Nemoto K, Takemori N, Seki M, Shinozaki K, Sawasaki T. Members of the plant CRK superfamily are capable of trans- and autophosphorylation of tyrosine residues. J Biol Chem. 2015;290:16665–16677. doi:https://doi.org/10.1074/jbc.M114.617274.
- Furumoto T, Ogawa N, Hata S, Izui K. Plant calcium-dependent protein kinase-related kinases (CRKs) do not require calcium for their activities. FEBS Lett. 1996;396:147–151. doi:https://doi.org/10.1016/0014-5793(96)01090-3.
- Harmon AC, Gribskov M, Harper JF. CDPKs-a kinase for every Ca2+ signal? Trends Plant Sci. 2000;5:154–159. doi:https://doi.org/10.1016/s1360-1385(00)01577-6.
- Baba AI, Rigo G, Ayaydin F, Rehman AU, Andrasi N, Zsigmond L, Valkai I, Urbancsok J, Vass I, Pasternak T, et al. Functional analysis of the Arabidopsis thaliana CDPK-related kinase family: atCRK1 regulates responses to continuous light. Int J Mol Sci. 2018;19:1282. doi:https://doi.org/10.3390/ijms19051282.
- Leclercq J, Ranty B, Sanchez-Ballesta MT, Li ZG, Jones B, Jauneau A, Pech JC, Latche A, Ranjeva R, Bouzayen M. Molecular and biochemical characterization of LeCRK1, a ripening associated tomato CDPK-related kinase. J Exp Bot. 2005;56:25–35. doi:https://doi.org/10.1093/jxb/eri003.
- Li RJ, Hua W, Lu YT. Arabidopsis cytosolic glutamine synthetase AtGLN1;1 is a potential substrate of AtCRK3 involved in leaf senescence. Biochem Bioph Res Co. 2006;342:119–126. doi:https://doi.org/10.1016/j.bbrc.2006.01.100.
- Liu HT, Gao F, Li GL, Han JL, Liu DL, Sun DY, Zhou RG. The calmodulin-binding protein kinase 3 is part of heat-shock signal transduction in Arabidopsis thaliana. Plant J. 2008;55:760–773. doi:https://doi.org/10.1111/j.1365-313X.2008.03544.x.
- Rigo G, Ayaydin F, Tietz O, Zsigmond L, Kovacs H, Pay A, Salchert K, Darula Z, Medzihradszky KF, Szabados L, et al. Inactivation of plasma membrane-localized CDPK-RELATED KINASE 5 decelerates PIN2 exocytosis and root gravitropic response in Arabidopsis. Plant Cell. 2013;25:1592–1608. doi:https://doi.org/10.1105/tpc.113.110452.
- Tao XC, Lu YT. Loss of AtCRK1 gene function in Arabidopsis thaliana decreases tolerance to salt. J Plant Biol. 2013;56:306–314. doi:https://doi.org/10.1007/s12374-012-0352-z.
- Baba AI, Andrasi N, Valkai I, Gorcsa T, Koczka L, Darula Z, Medzihradszky KF, Szabados L, Feher A, Rigo G, et al. AtCRK5 protein kinase exhibits a regulatory role in hypocotyl hook development during skotomorphogenesis. Int J Mol Sci. 2019a;20:3432. doi:https://doi.org/10.3390/ijms20143432.
- Baba AI, Valkai I, Labhane NM, Koczka L, Andrasi N, Klement E, Darula Z, Medzihradszky KF, Szabados L, Feher A, et al. CRK5 protein kinase contributes to the progression of embryogenesis of Arabidopsis thaliana. Int J Mol Sci. 2019b;20:6120. doi:https://doi.org/10.3390/ijms20246120.
- Zhang L, Bi-Feng LIU, Liang S, Jones RL, Ying-Tang LU. Molecular and biochemical characterization of a calcium/calmodulin-binding protein kinase from rice. Biochem J. 2002;368:145–157. doi:https://doi.org/10.1042/bj20020780.
- Neogy A, Garg T, Kumar A, Dwivedi AK, Singh H, Singh U, Singh Z, Prasad K, Jain M, Yadav SR. Genome-wide transcript profiling reveals an auxin-responsive transcription factor, OsAP2/ERF-40, promoting rice adventitious root development. Plant Cell Physiol. 2019;60:2343–2355. doi:https://doi.org/10.1093/pcp/pcz132.
- Prasad K, Parameswaran S, Vijayraghavan U. OsMADS1, a rice MADS box factor, controls differentiation of specific cell types in the lemma and palea and is an early acting regulator of inner floral organs. Plant J. 2005;43:915–928. doi:https://doi.org/10.1111/j.1365-313X.2005.02504.x.
- Yadav SR, Prasad K, Vijayraghavan U. Divergent regulatory OsMADS2 functions control size, shape and differentiation of the highly derived rice floret second-whorl organ. Genetics. 2007;176:283–294. doi:https://doi.org/10.1534/genetics.107.071746.
- Michniewicz M, Zago MK, Abas L, Weijers D, Schweighofer A, Meskiene I, Heisler MG, Ohno C, Zhang J, Huang F, et al. Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs auxin flux. Cell. 2007;130:1044–1056. doi:https://doi.org/10.1016/j.cell.2007.07.033.
- Barbosa IC, Hammes UZ, Schwechheimer C. Activation and polarity control of PIN-FORMED auxin transporters by phosphorylation. Trends Plant Sci. 2018;23:523–538. doi:https://doi.org/10.1016/j.tplants.2018.03.009.
- Du L, Jiao F, Chu J, Jin G, Chen M, Wu P. The two-component signal system in rice (Oryza sativa L.): a genome-wide study of cytokinin signal perception and transduction. Genomics. 2007;89:697–707. doi:https://doi.org/10.1016/j.ygeno.2007.02.001.