Tumor Biology

, Volume 36, Issue 3, pp 1423–1428

Mutation-introduced dimerization of receptor tyrosine kinases: from protein structure aberrations to carcinogenesis


DOI: 10.1007/s13277-015-3287-4

Cite this article as:
Hu, H., Liu, Y. & Jiang, T. Tumor Biol. (2015) 36: 1423. doi:10.1007/s13277-015-3287-4


Cancer is the greatest challenge to human health in our era. Perturbations of receptor tyrosine kinase (RTK) function contribute to a large chunk of cancer etiology. Current evidence supports that mutations in RTKs mediate receptor dimerization and result in ligand-independent kinase activity and tumorigenesis, indicating that mutation-introduced receptor dimerization is a critical component of oncogenesis RTK mutations. However, there are no specialized reviews of this important principle. In the current review, we discuss the physiological and harmless RTK function and subsequently examine mutation-introduced dimerization of RTKs and the role of these mutations in tumorigenesis. We also summarize the protein structure characteristics that are important for dimerization and introduce research methods and tools to predict and validate the existence of oncogenic mutations introduced by dimerization in RTKs.


Receptor tyrosine kinases Mutation Dimerization Oncogenicity Gene rearrangement Protein structure alteration Oncogenesis 

Copyright information

© International Society of Oncology and BioMarkers (ISOBM) 2015

Authors and Affiliations

  1. 1.Department of Molecular Neuropathology, Beijing Neurosurgical InstituteCapital Medical UniversityBeijingPeople’s Republic of China
  2. 2.Chinese Glioma Cooperative Group (CGCG)BeijingChina
  3. 3.Department of Neurosurgery, Beijing Tiantan HospitalCapital Medical UniversityBeijingPeople’s Republic of China
  4. 4.Beijing Institute for Brain Disorders Brain Tumor CenterBeijingChina

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