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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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SLK_HUMAN (a), MAST_HUMAN (b) and STK6_HUMAN (c) kinase domain architecture. S_TKc - catalytic domain of serine/threonine-kinases; S_TK_X - auxiliary S_TKc domain; DUF1908 - domain of unknown function (DUF1908); PDZ (also referred as DHR (Dlg homology region) or GLGF (relatively well conserved tetrapeptide in these domains) - domain found in PSD-95, Dlg and ZO-1/2[74]. These domains help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes [72].
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Figure 1: SLK_HUMAN (a), MAST_HUMAN (b) and STK6_HUMAN (c) kinase domain architecture. S_TKc - catalytic domain of serine/threonine-kinases; S_TK_X - auxiliary S_TKc domain; DUF1908 - domain of unknown function (DUF1908); PDZ (also referred as DHR (Dlg homology region) or GLGF (relatively well conserved tetrapeptide in these domains) - domain found in PSD-95, Dlg and ZO-1/2[74]. These domains help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes [72].

Mentions: Using public databases and published research papers [28-47], we have selected a range of human kinases involved in microtubule proteins phosphorylation and cell division regulation (Table 1). Depending on the complexity level of protein kinases domain organization, either full sequences (in case of AURKA) or catalytic domain sequence (SLK, PAK7, MARK1, SLK, MAST2 TTBK1, PLK1, PLK4 and PASK, as seen on Figure 1) were used for SIB BLASTp scanning. As a result of the UniProt database scanning, we identified plant homologues of human kinases from the families SLK, MAST2 and AURKA.


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)

SLK_HUMAN (a), MAST_HUMAN (b) and STK6_HUMAN (c) kinase domain architecture. S_TKc - catalytic domain of serine/threonine-kinases; S_TK_X - auxiliary S_TKc domain; DUF1908 - domain of unknown function (DUF1908); PDZ (also referred as DHR (Dlg homology region) or GLGF (relatively well conserved tetrapeptide in these domains) - domain found in PSD-95, Dlg and ZO-1/2[74]. These domains help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes [72].
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 1: SLK_HUMAN (a), MAST_HUMAN (b) and STK6_HUMAN (c) kinase domain architecture. S_TKc - catalytic domain of serine/threonine-kinases; S_TK_X - auxiliary S_TKc domain; DUF1908 - domain of unknown function (DUF1908); PDZ (also referred as DHR (Dlg homology region) or GLGF (relatively well conserved tetrapeptide in these domains) - domain found in PSD-95, Dlg and ZO-1/2[74]. These domains help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes [72].
Mentions: Using public databases and published research papers [28-47], we have selected a range of human kinases involved in microtubule proteins phosphorylation and cell division regulation (Table 1). Depending on the complexity level of protein kinases domain organization, either full sequences (in case of AURKA) or catalytic domain sequence (SLK, PAK7, MARK1, SLK, MAST2 TTBK1, PLK1, PLK4 and PASK, as seen on Figure 1) were used for SIB BLASTp scanning. As a result of the UniProt database scanning, we identified plant homologues of human kinases from the families SLK, MAST2 and AURKA.

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