Berezko desordenaren funtzioa CBP/p300 eta Miokardinaren arteko elkarrekintzan

Authors

  • Maddi Olaetxea Usabiaga University of the Basque Country (UPV/EHU)
  • Matthew Fishman Queen’s University, Kingston, ON, Kanada
  • Holly Spencer Queen’s University, Kingston, ON, Kanada
  • Steven Smith Queen’s University, Kingston, ON, Kanada

DOI:

https://doi.org/10.26876/ikergazte.vi.05.33

Keywords:

Intrinsically disordered proteins/regions (IDP/IDR), CREB binding protein (CBP/p300, Myocardin (MYOCD), Φ-X-X-Φ-Φ motif, isothermal titration calorimetry (ITC)

Abstract

Intrinsically disordered proteins lack a stable structure and hence can interact with multiple partners, a property critical for signaling and gene regulation. CBP/p300, a central acetyltransferase coactivator, interacts with transcription factors employing its structured motifs, generally identifying disordered Φ-X-X-Φ-Φ motifs in their transactivation domains. Myocardin, a critical TF for cardiac and vascular smooth muscle differentiation, is thought to bind to CBP/p300 via two such motifs.

Downloads

Published

2025-05-30

How to Cite

Olaetxea Usabiaga, M., Fishman, M., Spencer, H., & Smith, S. (2025). Berezko desordenaren funtzioa CBP/p300 eta Miokardinaren arteko elkarrekintzan. IkerGazte. Nazioarteko Ikerketa Euskaraz, 5, 267–274. https://doi.org/10.26876/ikergazte.vi.05.33