The Bardet-Biedl syndrome complex component BBS1 controls T cell polarity during immune synapse assembly

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F21%3A00554522" target="_blank" >RIV/68378050:_____/21:00554522 - isvavai.cz</a>

Výsledek na webu

<a href="https://journals.biologists.com/jcs/article/134/16/jcs258462/271909/The-Bardet-Biedl-syndrome-complex-component-BBS1" target="_blank" >https://journals.biologists.com/jcs/article/134/16/jcs258462/271909/The-Bardet-Biedl-syndrome-complex-component-BBS1</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1242/jcs.258462" target="_blank" >10.1242/jcs.258462</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The Bardet-Biedl syndrome complex component BBS1 controls T cell polarity during immune synapse assembly

Popis výsledku v původním jazyce

Components of the intraflagellar transport (IFT) system that regulates the assembly of the primary cilium are co-opted by the non-ciliated T cell to orchestrate polarized endosome recycling and to sustain signaling during immune synapse formation. Here, we investigated the potential role of Bardet-Biedl syndrome 1 protein (BBS1), an essential core component of the BBS complex that cooperates with the IFT system in ciliary protein trafficking, in the assembly of the T cell synapse. We demonstrated that BBS1 allows for centrosome polarization towards the immune synapse. This function is achieved through the clearance of centrosomal F-actin and its positive regulator WASH1 (also known as WASHC1), a process that we demonstrated to be dependent on the proteasome. We show that BBS1 regulates this process by coupling the 19S proteasome regulatory subunit to the microtubule motor dynein for its transport to the centrosome. Our data identify the ciliopathy-related protein BBS1 as a new player in T cell synapse assembly that functions upstream of the IFT system to set the stage for polarized vesicular trafficking and sustained signaling.

Název v anglickém jazyce

The Bardet-Biedl syndrome complex component BBS1 controls T cell polarity during immune synapse assembly

Popis výsledku anglicky

Components of the intraflagellar transport (IFT) system that regulates the assembly of the primary cilium are co-opted by the non-ciliated T cell to orchestrate polarized endosome recycling and to sustain signaling during immune synapse formation. Here, we investigated the potential role of Bardet-Biedl syndrome 1 protein (BBS1), an essential core component of the BBS complex that cooperates with the IFT system in ciliary protein trafficking, in the assembly of the T cell synapse. We demonstrated that BBS1 allows for centrosome polarization towards the immune synapse. This function is achieved through the clearance of centrosomal F-actin and its positive regulator WASH1 (also known as WASHC1), a process that we demonstrated to be dependent on the proteasome. We show that BBS1 regulates this process by coupling the 19S proteasome regulatory subunit to the microtubule motor dynein for its transport to the centrosome. Our data identify the ciliopathy-related protein BBS1 as a new player in T cell synapse assembly that functions upstream of the IFT system to set the stage for polarized vesicular trafficking and sustained signaling.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

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OECD FORD obor

10601 - Cell biology

Projekt

<a href="/cs/project/GJ19-03435Y" target="_blank" >GJ19-03435Y: Naivní, paměťové a virtuální paměťové buňky v adaptivních imunitních odpovědích</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2021

Kód důvěrnosti údajů

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

Název periodika

Journal of Cell Science

ISSN

0021-9533

e-ISSN

1477-9137

Svazek periodika

134

Číslo periodika v rámci svazku

16

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

18

Strana od-do

jcs258462

Kód UT WoS článku

000692211500011

EID výsledku v databázi Scopus

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