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Updated: May 16, 2026
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Dab1 stabilizes its interaction with Cin85 by suppressing Cin85 phosphorylation at serine 587
1Department of Biology, University of Vermont, Burlington, VT 05405, USA.
FEBS Letters
|November 27, 2012
Summary
Dab1 protein suppresses Cin85 phosphorylation, impacting neuronal positioning. This discovery sheds light on how Cin85
Area of Science:
- Neuroscience
- Cell Biology
- Molecular Biology
Background:
- Crk and CrkL adaptors are crucial for neuronal positioning, acting downstream of Reelin signaling.
- Cin85 is identified as a binding partner for CrkL and directly interacts with Dab1.
Purpose of the Study:
- To investigate the regulatory mechanism of Cin85 phosphorylation by Dab1.
- To understand how Dab1-Cin85 interaction influences neuronal positioning and cellular processes.
Main Methods:
- Mass spectrometry
- Biochemical assays
- Mutational analysis
Main Results:
- Dab1 was found to suppress Cin85 phosphorylation at Ser587.
- A phosphomimetic mutation at Cin85 Ser587 disrupted the Dab1-Cin85 complex.
- The Cin85 Ser587 phosphomimetic mutation did not affect the Cin85-CapZ complex.
Conclusions:
- Cin85 phosphorylation by Dab1 is a key regulatory event.
- Altered Cin85 phosphorylation may change its binding partners, affecting its roles in trafficking, endocytosis, and actin remodeling.
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