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The multi-functional eyes absent proteins.

Rashmi S Hegde1, Kaushik Roychoudhury1, Ram Naresh Pandey1

  • 1Division of Developmental Biology, Cincinnati Children's Hospital Research Foundation, Department of Pediatrics, University of Cincinnati School of Medicine, Cincinnati, OH, USA.

Critical Reviews in Biochemistry and Molecular Biology
|July 31, 2020
PubMed
Summary
This summary is machine-generated.

Eyes Absent (EYA) proteins possess unique tyrosine phosphatase, threonine phosphatase, and transactivation activities. Understanding these EYA functions is crucial for exploring their roles in development, disease, and potential therapeutic targeting.

Keywords:
DNA damage repairEYAEyes AbsentH2AXMYCNotchPTPthreonine phosphatase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Eyes Absent (EYA) proteins uniquely integrate tyrosine phosphatase, threonine phosphatase, and transactivation functions within a single polypeptide.
  • This multifunctional nature complicates the elucidation of specific biological roles for each activity.
  • EYA proteins are implicated in critical developmental processes and various pathological conditions.

Purpose of the Study:

  • To review the biochemical activities of Eyes Absent (EYA) proteins, focusing on their phosphatase activities.
  • To explore the interplay between EYA's phosphatase activities and its transactivation function.
  • To discuss the implications of EYA functions in disease states and the potential for therapeutic targeting.

Main Methods:

  • Review of existing literature on EYA protein functions.
  • Analysis of substrates and signaling pathways affected by EYA tyrosine phosphatase activity.
  • Examination of regulatory mechanisms and signaling pathways involving EYA threonine phosphatase activity.

Main Results:

  • EYA proteins participate in both transcriptional regulation and signal transduction pathways.
  • Emerging evidence links EYA activities to developmental and pathological functions.
  • Specific substrates and signaling pathways modulated by EYA tyrosine and threonine phosphatase activities are being identified.

Conclusions:

  • The dual phosphatase and transactivation activities of EYA proteins offer unique possibilities for biological regulation.
  • Further research into EYA functions is essential for understanding their roles in signaling cascades like MYC and Notch.
  • Targeting individual EYA activities presents a promising avenue for developing novel therapeutics for associated diseases.