Grb10 is a dual regulator of receptor tyrosine kinase signaling

Nuzhat N. Kabir; Julhash U. Kazi

doi:10.1007/s11033-014-3046-4

Grb10 is a dual regulator of receptor tyrosine kinase signaling

Nuzhat N. Kabir, Julhash U. Kazi

Department of Translational Medicine

Research output: Contribution to journal › Review article › peer-review

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Abstract

The adaptor protein Grb10 is a close homolog of Grb7 and Grb14. These proteins are characterized by an N-terminal proline-rich region, a Ras–GTPase binding domain, a PH domain, an SH2 domain and a BPS domain in between the PH and SH2 domains. Human Grb10 gene encodes three splice variants. These variants show differences in functionality. Grb10 associates with multiple proteins including tyrosine kinases in a tyrosine phosphorylation dependent or independent manner. Association with multiple proteins allows Grb10 to regulate different signaling pathways resulting in different biological consequences.

Original language	English
Pages (from-to)	1985-1992
Journal	Molecular Biology Reports
Volume	41
Issue number	4
DOIs	https://doi.org/10.1007/s11033-014-3046-4
Publication status	Published - 2014

Bibliographical note

The information about affiliations in this record was updated in December 2015.
The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)

Subject classification (UKÄ)

Medicinal Chemistry

Free keywords

InsR IGF-1R FLT3 KIT PDGFR VEGFR RTK Adaptor

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10.1007/s11033-014-3046-4

Springer__Kabir_et_al

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title = "Grb10 is a dual regulator of receptor tyrosine kinase signaling",

abstract = "The adaptor protein Grb10 is a close homolog of Grb7 and Grb14. These proteins are characterized by an N-terminal proline-rich region, a Ras–GTPase binding domain, a PH domain, an SH2 domain and a BPS domain in between the PH and SH2 domains. Human Grb10 gene encodes three splice variants. These variants show differences in functionality. Grb10 associates with multiple proteins including tyrosine kinases in a tyrosine phosphorylation dependent or independent manner. Association with multiple proteins allows Grb10 to regulate different signaling pathways resulting in different biological consequences.",

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AU - Kazi, Julhash U.

N1 - The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)

PY - 2014

Y1 - 2014

N2 - The adaptor protein Grb10 is a close homolog of Grb7 and Grb14. These proteins are characterized by an N-terminal proline-rich region, a Ras–GTPase binding domain, a PH domain, an SH2 domain and a BPS domain in between the PH and SH2 domains. Human Grb10 gene encodes three splice variants. These variants show differences in functionality. Grb10 associates with multiple proteins including tyrosine kinases in a tyrosine phosphorylation dependent or independent manner. Association with multiple proteins allows Grb10 to regulate different signaling pathways resulting in different biological consequences.

AB - The adaptor protein Grb10 is a close homolog of Grb7 and Grb14. These proteins are characterized by an N-terminal proline-rich region, a Ras–GTPase binding domain, a PH domain, an SH2 domain and a BPS domain in between the PH and SH2 domains. Human Grb10 gene encodes three splice variants. These variants show differences in functionality. Grb10 associates with multiple proteins including tyrosine kinases in a tyrosine phosphorylation dependent or independent manner. Association with multiple proteins allows Grb10 to regulate different signaling pathways resulting in different biological consequences.

KW - InsR IGF-1R FLT3 KIT PDGFR VEGFR RTK Adaptor

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DO - 10.1007/s11033-014-3046-4

M3 - Review article

C2 - 24420853

SN - 0301-4851

VL - 41

SP - 1985

EP - 1992

JO - Molecular Biology Reports

JF - Molecular Biology Reports

IS - 4

ER -

Grb10 is a dual regulator of receptor tyrosine kinase signaling

Abstract

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