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Bioinformatic search of plant microtubule-and cell cycle related serine-threonine protein kinases.

Karpov PA, Nadezhdina ES, Yemets AI, Matusov VG, Nyporko AY, Shashina NY, Blume YB - BMC Genomics (2010)

Bottom Line: A number of SLK, MAST2 and AURKA plant homologues were identified.The closest identified homologue of human AURKA kinase was a protein of unknown function, A7PY12/GSVIVT00026259001 from Vitis vinifera (herein named as "STALK", Serine-Threonine Aurora-Like Kinase).Analysis of STALK's three-dimensional structure confirmed its relationship to the subgroup of AURKA-like protein kinases.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, Kyiv, Ukraine. karpov.p.a@gmail.com

ABSTRACT
A bioinformatic search was carried for plant homologues of human serine-threonine protein kinases involved in regulation of cell division and microtubule protein phosphorylation (SLK, PAK6, PAK7, MARK1, MAST2, TTBK1, TTBK2, AURKA, PLK1, PLK4 and PASK). A number of SLK, MAST2 and AURKA plant homologues were identified. The closest identified homologue of human AURKA kinase was a protein of unknown function, A7PY12/GSVIVT00026259001 from Vitis vinifera (herein named as "STALK", Serine-Threonine Aurora-Like Kinase). Analysis of STALK's three-dimensional structure confirmed its relationship to the subgroup of AURKA-like protein kinases.

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Interplay of Plk1, AURKA and BORA in cell cycle based on literature data: adapted from [43,46]and is based on references [29,38,43,44,46,57].
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Figure 11: Interplay of Plk1, AURKA and BORA in cell cycle based on literature data: adapted from [43,46]and is based on references [29,38,43,44,46,57].

Mentions: An example of the corresponding homologue is Aurora A, a kinase responsible for daughter centrosome formation, asymmetric cell division and mitotic spindle formation [46]. It is believed that the signal from the cyclin-dependent kinase Cdk1 is relayed to the "second" level kinases, one of which is Aurora A [38,46]. In human and animal cells alike, AURKA (Aurora kinase A) is involved in the initiation of mitosis [30]. Activation of AURKA occurs by means of AURKA - BORA (protein BORA, FLJ22624; RP11-342J4.2; C13orf34) complex formation [29,38,43,57]. A mechanism was suggested recently, according to which BORA and AURKA together control transition from phase G2 of cell cycle to phase M [44]. According to the proposed mechanism, Cdk1 causes BORA to exit from the nucleus and binds reversibly with Plk1. This changes Plk1 conformation so that its Thr210 in the catalytic domain becomes accessible for phosphorylation by AURKA with subsequent Plk1 activation [44]. This leads to further Cdk1 activation, degradation of Bora and, eventually, to start of mitosis [44,46] (Figure 11).


Bioinformatic search of plant microtubule-and cell cycle related serine-threonine protein kinases.

Karpov PA, Nadezhdina ES, Yemets AI, Matusov VG, Nyporko AY, Shashina NY, Blume YB - BMC Genomics (2010)

Interplay of Plk1, AURKA and BORA in cell cycle based on literature data: adapted from [43,46]and is based on references [29,38,43,44,46,57].
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2822528&req=5

Figure 11: Interplay of Plk1, AURKA and BORA in cell cycle based on literature data: adapted from [43,46]and is based on references [29,38,43,44,46,57].
Mentions: An example of the corresponding homologue is Aurora A, a kinase responsible for daughter centrosome formation, asymmetric cell division and mitotic spindle formation [46]. It is believed that the signal from the cyclin-dependent kinase Cdk1 is relayed to the "second" level kinases, one of which is Aurora A [38,46]. In human and animal cells alike, AURKA (Aurora kinase A) is involved in the initiation of mitosis [30]. Activation of AURKA occurs by means of AURKA - BORA (protein BORA, FLJ22624; RP11-342J4.2; C13orf34) complex formation [29,38,43,57]. A mechanism was suggested recently, according to which BORA and AURKA together control transition from phase G2 of cell cycle to phase M [44]. According to the proposed mechanism, Cdk1 causes BORA to exit from the nucleus and binds reversibly with Plk1. This changes Plk1 conformation so that its Thr210 in the catalytic domain becomes accessible for phosphorylation by AURKA with subsequent Plk1 activation [44]. This leads to further Cdk1 activation, degradation of Bora and, eventually, to start of mitosis [44,46] (Figure 11).

Bottom Line: A number of SLK, MAST2 and AURKA plant homologues were identified.The closest identified homologue of human AURKA kinase was a protein of unknown function, A7PY12/GSVIVT00026259001 from Vitis vinifera (herein named as "STALK", Serine-Threonine Aurora-Like Kinase).Analysis of STALK's three-dimensional structure confirmed its relationship to the subgroup of AURKA-like protein kinases.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, Kyiv, Ukraine. karpov.p.a@gmail.com

ABSTRACT
A bioinformatic search was carried for plant homologues of human serine-threonine protein kinases involved in regulation of cell division and microtubule protein phosphorylation (SLK, PAK6, PAK7, MARK1, MAST2, TTBK1, TTBK2, AURKA, PLK1, PLK4 and PASK). A number of SLK, MAST2 and AURKA plant homologues were identified. The closest identified homologue of human AURKA kinase was a protein of unknown function, A7PY12/GSVIVT00026259001 from Vitis vinifera (herein named as "STALK", Serine-Threonine Aurora-Like Kinase). Analysis of STALK's three-dimensional structure confirmed its relationship to the subgroup of AURKA-like protein kinases.

Show MeSH