Caspase Cleavage of Receptor Tyrosine Kinases in the Dependence Receptor Family

Dependence receptors are a group of receptor proteins with shared characteristics of transducing two different signals within cells. They can transduce a positive signal of survival and differentiation in the presence of ligands. On the other hand, dependence receptors can transduce an apoptosis sig...

Full description

Saved in:
Bibliographic Details
Published inBiomolecules & therapeutics Vol. 31; no. 4; pp. 359 - 369
Main Authors Park, Gyu Hwan, Kang, Yoo Kyung, Paek, Seung-Mann, Shin, Chan Young, Han, Sun-Young
Format Journal Article
LanguageEnglish
Published Korea (South) The Korean Society of Applied Pharmacology 01.07.2023
Subjects
Review
Caspase
Receptor tyrosine kinase
Cleavage
Dependence receptor
Online AccessGet full text

Cover

More Information
Summary:Dependence receptors are a group of receptor proteins with shared characteristics of transducing two different signals within cells. They can transduce a positive signal of survival and differentiation in the presence of ligands. On the other hand, dependence receptors can transduce an apoptosis signal in the absence of ligands. The function of these receptors depends on the availability of their ligands. Several receptor tyrosine kinases (RTKs) have been reported as dependence receptors. When cells undergo apoptosis by dependence receptors, the intracellular domain of some RTKs is cleaved by the caspases. Among the RTKs that belong to dependence receptors, we focused on eight RTKs (RET, HER2, MET, ALK, TrkC, EphA4, EphB3, and c-KIT) that are cleaved by caspases. In this review, we describe the features of the receptors, their cleavage sites, and the fate of the cleaved products, as well as recent implications on them being used as potential therapeutics for cancer treatment.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
The first two authors contributed equally to this work.
ISSN:1976-9148
2005-4483
DOI:10.4062/biomolther.2022.133