Characterization of the C-terminal domain of ras-GTPase-activating protein (ras-GAP) as substrate for epidermal growth factor receptor and p60c-src kinase.

P Borowski; L Kornetzky; M Heiland; S Roloff; Wolfgang Weber; R Laufs

Characterization of the C-terminal domain of ras-GTPase-activating protein (ras-GAP) as substrate for epidermal growth factor receptor and p60c-src kinase.

Standard

Characterization of the C-terminal domain of ras-GTPase-activating protein (ras-GAP) as substrate for epidermal growth factor receptor and p60c-src kinase. / Borowski, P; Kornetzky, L; Heiland, M; Roloff, S; Weber, Wolfgang; Laufs, R.

in: Biochem Mol Biol Int, Jahrgang 39, Nr. 3, 3, 1996, S. 635-646.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Borowski, P, Kornetzky, L, Heiland, M, Roloff, S, Weber, W & Laufs, R 1996, 'Characterization of the C-terminal domain of ras-GTPase-activating protein (ras-GAP) as substrate for epidermal growth factor receptor and p60c-src kinase.', Biochem Mol Biol Int, Jg. 39, Nr. 3, 3, S. 635-646. <http://www.ncbi.nlm.nih.gov/pubmed/8828816?dopt=Citation>

APA

Borowski, P., Kornetzky, L., Heiland, M., Roloff, S., Weber, W., & Laufs, R. (1996). Characterization of the C-terminal domain of ras-GTPase-activating protein (ras-GAP) as substrate for epidermal growth factor receptor and p60c-src kinase. Biochem Mol Biol Int, 39(3), 635-646. [3]. http://www.ncbi.nlm.nih.gov/pubmed/8828816?dopt=Citation

Vancouver

Borowski P, Kornetzky L, Heiland M, Roloff S, Weber W, Laufs R. Characterization of the C-terminal domain of ras-GTPase-activating protein (ras-GAP) as substrate for epidermal growth factor receptor and p60c-src kinase. Biochem Mol Biol Int. 1996;39(3):635-646. 3.

Bibtex

@article{893acde4e5f44665a42f5050d880f98f,

title = "Characterization of the C-terminal domain of ras-GTPase-activating protein (ras-GAP) as substrate for epidermal growth factor receptor and p60c-src kinase.",

abstract = "We describe in vitro tyrosine phosphorylation of the C-terminal 334 amino acids of ras-GTPase-activating protein (ras-GAP)1 that contains the activity domain for ras interaction. To date, there have been no other phosphorylation sites determined than the reported in N-terminal domain of ras-GAP Tyr-460, which is considered to be the major phosphorylation site of ras-GAP. In our assays some differences of the kinetic parameters were observed when the reaction was catalyzed by EGF-R compared to p60c-src. Enzyme specific regulation of activity is associated with autophosphorylation which leads to reduced (in case of EGF-R) or increased (in case of p60c-src) phosphorylation of the C-terminal 334 amino acids of ras-GAP (GAP334). Because of the characteristics of these investigated reactions the phosphorylation of GAP334 seems to be-independent from the presence of SH2 or SH3 domains-triggered off by complex mechanisms different from those regulating the phosphorylation at Tyr-460.",

keywords = "Humans, Kinetics, Phosphorylation, Enzyme Activation, Tumor Cells, Cultured, Electrophoresis, Polyacrylamide Gel, Receptor, Epidermal Growth Factor/*metabolism, Proteins/chemistry/*metabolism, Trypsin/metabolism, GTPase-Activating Proteins, Histones/pharmacology, Magnesium/metabolism, Manganese/metabolism, Ovalbumin/pharmacology, Peptide Fragments/metabolism, Phosphopeptides/analysis/metabolism, Phosphoserine/analysis/metabolism, Phosphothreonine/analysis/metabolism, Phosphotyrosine/analysis/metabolism, Polyglutamic Acid/analogs & derivatives/pharmacology, Polylysine/analogs & derivatives/pharmacology, Tyrosine/metabolism, ras GTPase-Activating Proteins, src-Family Kinases/*metabolism, Humans, Kinetics, Phosphorylation, Enzyme Activation, Tumor Cells, Cultured, Electrophoresis, Polyacrylamide Gel, Receptor, Epidermal Growth Factor/*metabolism, Proteins/chemistry/*metabolism, Trypsin/metabolism, GTPase-Activating Proteins, Histones/pharmacology, Magnesium/metabolism, Manganese/metabolism, Ovalbumin/pharmacology, Peptide Fragments/metabolism, Phosphopeptides/analysis/metabolism, Phosphoserine/analysis/metabolism, Phosphothreonine/analysis/metabolism, Phosphotyrosine/analysis/metabolism, Polyglutamic Acid/analogs & derivatives/pharmacology, Polylysine/analogs & derivatives/pharmacology, Tyrosine/metabolism, ras GTPase-Activating Proteins, src-Family Kinases/*metabolism",

author = "P Borowski and L Kornetzky and M Heiland and S Roloff and Wolfgang Weber and R Laufs",

year = "1996",

language = "English",

volume = "39",

pages = "635--646",

number = "3",

}

RIS

TY - JOUR

T1 - Characterization of the C-terminal domain of ras-GTPase-activating protein (ras-GAP) as substrate for epidermal growth factor receptor and p60c-src kinase.

AU - Borowski, P

AU - Kornetzky, L

AU - Heiland, M

AU - Roloff, S

AU - Weber, Wolfgang

AU - Laufs, R

PY - 1996

Y1 - 1996

N2 - We describe in vitro tyrosine phosphorylation of the C-terminal 334 amino acids of ras-GTPase-activating protein (ras-GAP)1 that contains the activity domain for ras interaction. To date, there have been no other phosphorylation sites determined than the reported in N-terminal domain of ras-GAP Tyr-460, which is considered to be the major phosphorylation site of ras-GAP. In our assays some differences of the kinetic parameters were observed when the reaction was catalyzed by EGF-R compared to p60c-src. Enzyme specific regulation of activity is associated with autophosphorylation which leads to reduced (in case of EGF-R) or increased (in case of p60c-src) phosphorylation of the C-terminal 334 amino acids of ras-GAP (GAP334). Because of the characteristics of these investigated reactions the phosphorylation of GAP334 seems to be-independent from the presence of SH2 or SH3 domains-triggered off by complex mechanisms different from those regulating the phosphorylation at Tyr-460.

AB - We describe in vitro tyrosine phosphorylation of the C-terminal 334 amino acids of ras-GTPase-activating protein (ras-GAP)1 that contains the activity domain for ras interaction. To date, there have been no other phosphorylation sites determined than the reported in N-terminal domain of ras-GAP Tyr-460, which is considered to be the major phosphorylation site of ras-GAP. In our assays some differences of the kinetic parameters were observed when the reaction was catalyzed by EGF-R compared to p60c-src. Enzyme specific regulation of activity is associated with autophosphorylation which leads to reduced (in case of EGF-R) or increased (in case of p60c-src) phosphorylation of the C-terminal 334 amino acids of ras-GAP (GAP334). Because of the characteristics of these investigated reactions the phosphorylation of GAP334 seems to be-independent from the presence of SH2 or SH3 domains-triggered off by complex mechanisms different from those regulating the phosphorylation at Tyr-460.

KW - Humans

KW - Kinetics

KW - Phosphorylation

KW - Enzyme Activation

KW - Tumor Cells, Cultured

KW - Electrophoresis, Polyacrylamide Gel

KW - Receptor, Epidermal Growth Factor/metabolism

KW - Proteins/chemistry/metabolism

KW - Trypsin/metabolism

KW - GTPase-Activating Proteins

KW - Histones/pharmacology

KW - Magnesium/metabolism

KW - Manganese/metabolism

KW - Ovalbumin/pharmacology

KW - Peptide Fragments/metabolism

KW - Phosphopeptides/analysis/metabolism

KW - Phosphoserine/analysis/metabolism

KW - Phosphothreonine/analysis/metabolism

KW - Phosphotyrosine/analysis/metabolism

KW - Polyglutamic Acid/analogs & derivatives/pharmacology

KW - Polylysine/analogs & derivatives/pharmacology

KW - Tyrosine/metabolism

KW - ras GTPase-Activating Proteins

KW - src-Family Kinases/metabolism