HSBP1 Is a Novel Interactor of FIP200 and ATG13 That Promotes Autophagy Initiation and Picornavirus Replication

ATG13 and FIP200 are two subunits of the ULK kinase complex, a key regulatory component of the autophagy machinery. We have previously found that the FIP200-ATG13 subcomplex controls picornavirus replication outside its role in the ULK kinase complex and autophagy. Here, we characterized HSBP1, a ve...

Full description

Saved in:

Bibliographic Details
Main Authors:	Mario Mauthe, Nilima Dinesh Kumar, Pauline Verlhac, Nicole van de Beek, Fulvio Reggiori
Format:	article
Language:	EN
Published:	Frontiers Media S.A. 2021
Subjects:	autophagy infection ULK kinase complex EMCV CVB3 EV71 Microbiology QR1-502
Online Access:	https://doaj.org/article/2e60091d0ac04ee3befcce4a0197e6b9
Tags:	Add Tag No Tags, Be the first to tag this record!

id	oai:doaj.org-article:2e60091d0ac04ee3befcce4a0197e6b9
record_format	dspace
spelling	oai:doaj.org-article:2e60091d0ac04ee3befcce4a0197e6b92021-11-15T06:05:48ZHSBP1 Is a Novel Interactor of FIP200 and ATG13 That Promotes Autophagy Initiation and Picornavirus Replication2235-298810.3389/fcimb.2021.745640https://doaj.org/article/2e60091d0ac04ee3befcce4a0197e6b92021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fcimb.2021.745640/fullhttps://doaj.org/toc/2235-2988ATG13 and FIP200 are two subunits of the ULK kinase complex, a key regulatory component of the autophagy machinery. We have previously found that the FIP200-ATG13 subcomplex controls picornavirus replication outside its role in the ULK kinase complex and autophagy. Here, we characterized HSBP1, a very small cytoplasmic coiled-coil protein, as a novel interactor of FIP200 and ATG13 that binds these two proteins via FIP200. HSBP1 is a novel pro-picornaviral host factor since its knockdown or knockout, inhibits the replication of various picornaviruses. The anti-picornaviral function of the FIP200-ATG13 subcomplex was abolished when HSBP1 was depleted, inferring that this subcomplex negatively regulates HSBP1’s pro-picornaviral function during infections. HSBP1depletion also reduces the stability of ULK kinase complex subunits, resulting in an impairment in autophagy induction. Altogether, our data show that HSBP1 interaction with FIP200-ATG13-containing complexes is involved in the regulation of different cellular pathways.Mario MautheNilima Dinesh KumarNilima Dinesh KumarPauline VerlhacNicole van de BeekFulvio ReggioriFrontiers Media S.A.articleautophagyinfectionULK kinase complexEMCVCVB3EV71MicrobiologyQR1-502ENFrontiers in Cellular and Infection Microbiology, Vol 11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	autophagy infection ULK kinase complex EMCV CVB3 EV71 Microbiology QR1-502
spellingShingle	autophagy infection ULK kinase complex EMCV CVB3 EV71 Microbiology QR1-502 Mario Mauthe Nilima Dinesh Kumar Nilima Dinesh Kumar Pauline Verlhac Nicole van de Beek Fulvio Reggiori HSBP1 Is a Novel Interactor of FIP200 and ATG13 That Promotes Autophagy Initiation and Picornavirus Replication
description	ATG13 and FIP200 are two subunits of the ULK kinase complex, a key regulatory component of the autophagy machinery. We have previously found that the FIP200-ATG13 subcomplex controls picornavirus replication outside its role in the ULK kinase complex and autophagy. Here, we characterized HSBP1, a very small cytoplasmic coiled-coil protein, as a novel interactor of FIP200 and ATG13 that binds these two proteins via FIP200. HSBP1 is a novel pro-picornaviral host factor since its knockdown or knockout, inhibits the replication of various picornaviruses. The anti-picornaviral function of the FIP200-ATG13 subcomplex was abolished when HSBP1 was depleted, inferring that this subcomplex negatively regulates HSBP1’s pro-picornaviral function during infections. HSBP1depletion also reduces the stability of ULK kinase complex subunits, resulting in an impairment in autophagy induction. Altogether, our data show that HSBP1 interaction with FIP200-ATG13-containing complexes is involved in the regulation of different cellular pathways.
format	article
author	Mario Mauthe Nilima Dinesh Kumar Nilima Dinesh Kumar Pauline Verlhac Nicole van de Beek Fulvio Reggiori
author_facet	Mario Mauthe Nilima Dinesh Kumar Nilima Dinesh Kumar Pauline Verlhac Nicole van de Beek Fulvio Reggiori
author_sort	Mario Mauthe
title	HSBP1 Is a Novel Interactor of FIP200 and ATG13 That Promotes Autophagy Initiation and Picornavirus Replication
title_short	HSBP1 Is a Novel Interactor of FIP200 and ATG13 That Promotes Autophagy Initiation and Picornavirus Replication
title_full	HSBP1 Is a Novel Interactor of FIP200 and ATG13 That Promotes Autophagy Initiation and Picornavirus Replication
title_fullStr	HSBP1 Is a Novel Interactor of FIP200 and ATG13 That Promotes Autophagy Initiation and Picornavirus Replication
title_full_unstemmed	HSBP1 Is a Novel Interactor of FIP200 and ATG13 That Promotes Autophagy Initiation and Picornavirus Replication
title_sort	hsbp1 is a novel interactor of fip200 and atg13 that promotes autophagy initiation and picornavirus replication
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/2e60091d0ac04ee3befcce4a0197e6b9
work_keys_str_mv	AT mariomauthe hsbp1isanovelinteractoroffip200andatg13thatpromotesautophagyinitiationandpicornavirusreplication AT nilimadineshkumar hsbp1isanovelinteractoroffip200andatg13thatpromotesautophagyinitiationandpicornavirusreplication AT nilimadineshkumar hsbp1isanovelinteractoroffip200andatg13thatpromotesautophagyinitiationandpicornavirusreplication AT paulineverlhac hsbp1isanovelinteractoroffip200andatg13thatpromotesautophagyinitiationandpicornavirusreplication AT nicolevandebeek hsbp1isanovelinteractoroffip200andatg13thatpromotesautophagyinitiationandpicornavirusreplication AT fulvioreggiori hsbp1isanovelinteractoroffip200andatg13thatpromotesautophagyinitiationandpicornavirusreplication
_version_	1718428543445106688

HSBP1 Is a Novel Interactor of FIP200 and ATG13 That Promotes Autophagy Initiation and Picornavirus Replication

Similar Items