All Good Things Must End: Termination of Receptor Tyrosine Kinase Signal

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F21%3A00075112" target="_blank" >RIV/00159816:_____/21:00075112 - isvavai.cz</a>

Alternative codes found

RIV/00216224:14110/21:00124195

Result on the web

<a href="https://www.mdpi.com/1422-0067/22/12/6342/htm" target="_blank" >https://www.mdpi.com/1422-0067/22/12/6342/htm</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/ijms22126342" target="_blank" >10.3390/ijms22126342</a>

Result language

angličtina

Original language name

All Good Things Must End: Termination of Receptor Tyrosine Kinase Signal

Original language description

Receptor tyrosine kinases (RTKs) are membrane receptors that regulate many fundamental cellular processes. A tight regulation of RTK signaling is fundamental for development and survival, and an altered signaling by RTKs can cause cancer. RTKs are localized at the plasma membrane (PM) and the major regulatory mechanism of signaling of RTKs is their endocytosis and degradation. In fact, RTKs at the cell surface bind ligands with their extracellular domain, become active, and are rapidly internalized where the temporal extent of signaling, attenuation, and downregulation are modulated. However, other mechanisms of signal attenuation and termination are known. Indeed, inhibition of RTKs&apos; activity may occur through the modulation of the phosphorylation state of RTKs and the interaction with specific proteins, whereas antagonist ligands can inhibit the biological responses mediated by the receptor. Another mechanism concerns the expression of endogenous inactive receptor variants that are deficient in RTK activity and take part to inactive heterodimers or hetero-oligomers. The downregulation of RTK signals is fundamental for several cellular functions and the homeostasis of the cell. Here, we will review the mechanisms of signal attenuation and termination of RTKs, focusing on FGFRs.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2021

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

ISSN

1422-0067

e-ISSN

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Volume of the periodical

22

Issue of the periodical within the volume

12

Country of publishing house

CH - SWITZERLAND

Number of pages

14

Pages from-to

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UT code for WoS article

000665932000001

EID of the result in the Scopus database

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