Protein kinase recognition sequence motifs

Kemp, Bruce E.; Pearson, Richard B.

doi:10.1016/0968-0004(90)90073-k

Cited by 979 publications

(545 citation statements)

References 26 publications

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“…Although the spacing of these prolines does not precisely match the PXXP motif expected for molecules that bind to SH3 domains (Ren et al, 1993;Feng et al, 1994;Yu et al, 1994), we have preliminary evidence for the ability of NG2 to interact with the SH3 domains present in some types of cytoplasmic adapter molecules (our unpublished results). Finally, there are three threonine residues (Thr-2255, Thr-2264, and Thr-2277) in consensus sequences that could be substrates for phosphorylation by PKC and a fourth (Thr-2313) that could be phosphorylated by a proline-dependent kinase (Kemp and Pearson, 1990). The NG2/t3 mutant was created by terminating the NG2 protein at residue 2276, thereby eliminating the putative PDZ-binding domain, the proline-rich segment, and two of the potential phosphorylation sites.…”

Section: Discussionmentioning

confidence: 99%

Cytoskeletal Reorganization Induced by Engagement of the NG2 Proteoglycan Leads to Cell Spreading and Migration

Fang

Burg

Barritt

et al. 1999

MBoC

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Cells expressing the NG2 proteoglycan can attach, spread, and migrate on surfaces coated with NG2 mAbs, demonstrating that engagement of NG2 can trigger the cytoskeletal rearrangements necessary for changes in cell morphology and motility. Engagement of different epitopes of the proteoglycan results in distinct forms of actin reorganization. On mAb D120, the cells contain radial actin spikes characteristic of filopodial extension, whereas on mAb N143, the cells contain cortical actin bundles characteristic of lamellipodia. Cells that express NG2 variants lacking the transmembrane and cytoplasmic domains are unable to spread or migrate on NG2 mAb-coated surfaces, indicating that these portions of the molecule are essential for NG2-mediated signal transduction. Cells expressing an NG2 variant lacking the C-terminal half of the cytoplasmic domain can still spread normally on mAbs D120 and N143, suggesting that the membraneproximal cytoplasmic segment is responsible for this process. In contrast, this variant migrates poorly on mAb D120 and exhibits abnormal arrays of radial actin filaments decorated with fascin during spreading on this mAb. The C-terminal portion of the NG2 cytoplasmic domain, therefore, may be involved in regulating molecular events that are crucial for cell motility.

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Section: Discussionmentioning

confidence: 99%

Cytoskeletal Reorganization Induced by Engagement of the NG2 Proteoglycan Leads to Cell Spreading and Migration

Fang

Burg

Barritt

et al. 1999

MBoC

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“…Similarly, the 9-amino acids sequence (FENEENNRK, amino acids 12-20) of PEBP2fi which shows local homology with yeast heat-shock factor HSFl (Ogawa et al 1993a) is not conserved. Both Drosophila proteins contains several serine and threonine residues which may be recognized by protein kinases (Kemp & Pearson 1990). For example, both proteins have a putative phosphorylation site for CAMP dependent kinase, FRRLSR, which conforms to the proposed recognition motif X R R X S X for both the mammalian and yeast kinases (Kemp & Pearson 1990).…”

Section: Discussionmentioning

confidence: 99%

Runt domain partner proteins enhance DNA binding and transcriptional repression in cultured Drosophila cells

et al. 1996

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Background The Drosophila gene runt plays multiple roles during embryogenesis, including one as a pairrule class segmentation gene. The runt protein (Runt) contains an evolutionarily conserved domain (the Runt domain) that is found in several mammalian proteins including the human protein AMLI, which is involved in many chromosome translocations associated with leukaemia. Specific DNA binding activity of a mammalian Runt domain is enhanced

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“…This together with the inability to utilize GTP as a phosphoryl donor and to be inhibited by low concentrations of heparin indicate that these kinases may be classified as casein kinase I. Unlike casein kinase II, which recognizes a cluster of acidic amino acid residues at the C-terminal side of serine or threonine, casein kinase I has been suggested to prefer sites downstream from acidic sequences [23,24]. However, this requirement is not absolute.…”

Section: Discussionmentioning

confidence: 99%

Identity and substrate specificity of human erythrocyte membrane‐bound and cytosolic casein kinases

1991

FEBS Letters

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The relationship and substrate specificity of the human erythrocyte membrane kinase and casein kinase A were investigated. Based on Staphylococcus attreus V8 protease digestion patterns, the 2 kinases appeared to be structurally homologous. These enzymes also exhibited the same substrate specificity and phosphorylated the same synthetic peptides and domains of ankyrin. Both kinases did not utilize GTP effectively as a substrate and were not inhibited by low concentrations of heparin, suggesting that they were type I casein kinases. An analysis ofsynthetlc peptide phosphorylation failed to reveal a specific pattern of recognition of the amino acid sequence surrounding the phosphorylation site.

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Protein kinase recognition sequence motifs

Cited by 979 publications

References 26 publications

Cytoskeletal Reorganization Induced by Engagement of the NG2 Proteoglycan Leads to Cell Spreading and Migration

Cytoskeletal Reorganization Induced by Engagement of the NG2 Proteoglycan Leads to Cell Spreading and Migration

Runt domain partner proteins enhance DNA binding and transcriptional repression in cultured Drosophila cells

Identity and substrate specificity of human erythrocyte membrane‐bound and cytosolic casein kinases

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Protein kinase recognition sequence motifs

Cited by 979 publications

References 26 publications

Cytoskeletal Reorganization Induced by Engagement of the NG2 Proteoglycan Leads to Cell Spreading and Migration

Cytoskeletal Reorganization Induced by Engagement of the NG2 Proteoglycan Leads to Cell Spreading and Migration

Runt domain partner proteins enhance DNA binding and transcriptional repression in cultured Drosophila cells

Identity and substrate specificity of human erythrocyte membrane&#x2010;bound and cytosolic casein kinases

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Identity and substrate specificity of human erythrocyte membrane‐bound and cytosolic casein kinases