WBP1L, a transmembrane adaptor protein involved in the regulation of hematopoiesis, is controlled by CRL1 β _ TrCP ubiquitin ligases

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F25%3A00617135" target="_blank" >RIV/68378050:_____/25:00617135 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/25:10500891

Výsledek na webu

<a href="https://doi.org/10.1016/j.bbrc.2025.151337" target="_blank" >https://doi.org/10.1016/j.bbrc.2025.151337</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbrc.2025.151337" target="_blank" >10.1016/j.bbrc.2025.151337</a>

Jazyk výsledku

angličtina

Název v původním jazyce

WBP1L, a transmembrane adaptor protein involved in the regulation of hematopoiesis, is controlled by CRL1 β _ TrCP ubiquitin ligases

Popis výsledku v původním jazyce

WBP1L is a broadly expressed transmembrane adaptor protein involved in regulating hematopoietic stem cell function and T cell development. It interacts with NEDD4-family E3 ubiquitin ligases and regulates important chemokine receptor CXCR4. Using tandem affinity purification coupled with mass spectrometry, we identified novel WBP1L interactions with the IFN gamma receptor and the Cullin-RING ubiquitin ligases CRL1 beta _ TrCP1/2 . We found that WBP1L interaction with the IFN gamma receptor serves to downregulate proximal IFN gamma receptor signaling in female macrophages, while the interaction with CRL1 beta _ TrCP1/2 ubiquitin ligases regulates WBP1L protein levels. Disrupting this interaction, as well as inhibiting proteasome activity or neddylation, increased WBP1L protein levels, demonstrating that CRL1 beta _ TrCP1/2 ubiquitin ligases regulate WBP1L protein abundance. These data provide important insights into the mechanisms controlling WBP1L function.

Název v anglickém jazyce

WBP1L, a transmembrane adaptor protein involved in the regulation of hematopoiesis, is controlled by CRL1 β _ TrCP ubiquitin ligases

Popis výsledku anglicky

WBP1L is a broadly expressed transmembrane adaptor protein involved in regulating hematopoietic stem cell function and T cell development. It interacts with NEDD4-family E3 ubiquitin ligases and regulates important chemokine receptor CXCR4. Using tandem affinity purification coupled with mass spectrometry, we identified novel WBP1L interactions with the IFN gamma receptor and the Cullin-RING ubiquitin ligases CRL1 beta _ TrCP1/2 . We found that WBP1L interaction with the IFN gamma receptor serves to downregulate proximal IFN gamma receptor signaling in female macrophages, while the interaction with CRL1 beta _ TrCP1/2 ubiquitin ligases regulates WBP1L protein levels. Disrupting this interaction, as well as inhibiting proteasome activity or neddylation, increased WBP1L protein levels, demonstrating that CRL1 beta _ TrCP1/2 ubiquitin ligases regulate WBP1L protein abundance. These data provide important insights into the mechanisms controlling WBP1L function.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

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

Název periodika

Biochemical and Biophysical Research Communications

ISSN

0006-291X

e-ISSN

1090-2104

Svazek periodika

749

Číslo periodika v rámci svazku

16 Feb

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

151337

Kód UT WoS článku

001407855100001

EID výsledku v databázi Scopus

2-s2.0-85215211279