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Structure and function of SH2-domain containing tyrosine phosphatases
1Molecular Medicine Unit, Beth Israel Hospital, Boston, MA 02215.
Seminars in Cell Biology
|December 1, 1993
Summary
Protein tyrosine phosphatases (PTPases) with SH2 domains are crucial for growth factor signaling. This review details SH-PTP1 and SH-PTP2 roles in signal transduction and discusses genetic studies in mice and Drosophila.
Area of Science:
- Cellular signaling
- Molecular biology
- Biochemistry
Background:
- Tyrosyl phosphorylation is key in growth factor-receptor signaling.
- The precise roles of protein tyrosine phosphatases (PTPases) in these pathways remain unclear.
- SH2 domain-containing PTPases are likely involved in early signaling events.
Purpose of the Study:
- To review mammalian SH2-containing PTPases, SH-PTP1 and SH-PTP2.
- To discuss their potential roles in signal transduction pathways.
- To explore implications from genetic studies in model organisms.
Main Methods:
- Literature review of PTPase functions.
- Analysis of SH2 domain interactions with phosphotyrosyl proteins.
- Synthesis of findings from genetic studies in mouse and Drosophila.
Main Results:
- SH-PTP1 and SH-PTP2 are the two main mammalian SH2-containing PTPases.
- These PTPases are implicated in early signaling events after growth factor stimulation.
- Genetic studies provide insights into their physiological and pathological functions.
Conclusions:
- SH2-containing PTPases are significant regulators of signal transduction.
- Further research into SH-PTP1 and SH-PTP2 is warranted.
- Understanding these PTPases is crucial for comprehending cellular responses to growth factors.