HD-PTP and Alix share some membrane-traffic related proteins that interact with their Bro1 domains or proline-rich regions

Ichioka, Fumitaka, Takaya, Emi, Suzuki, Hironori, Kajigaya, Sachiko, Buchman, Vladimir L. ORCID: https://orcid.org/0000-0002-7631-8352, Shibata, Hideki and Maki, Masatoshi 2007. HD-PTP and Alix share some membrane-traffic related proteins that interact with their Bro1 domains or proline-rich regions. Archives of biochemistry and biophysics 457 (2) , pp. 142-149. 10.1016/j.abb.2006.11.008

Full text not available from this repository.

Abstract

Mammalian Alix is a multifunctional adaptor protein involved in cell death, receptor endocytosis, endosomal protein sorting and cell adhesion by associating with various proteins such as ALG-2, CIN85/Rukl/SETA, endophilins, CHMP4s and TSG101. HD-PTP is a paralog of Alix and a putative protein tyrosine phosphatase (PTP) that contains a Bro1 domain, coiled-coils, a proline-rich region (PRR) in addition to a PTP domain. We investigated interactions between HD-PTP and Alix-binding proteins. In the yeast two-hybrid assay, HD-PTP showed positive interactions with CHMP4b/Shax1, TSG101, endophilin A1 and ALG-2 but not with either RabGAPLP or CIN85. We confirmed the interactions in a mammalian system by Strep-pulldown assays in which pulldown products from the lysates of HEK293T cells expressing either Strep-tagged HD-PTP alone or co-expressing with epitope-tagged proteins were analyzed by Western blotting using specific antibodies. While Alix associated with both ALG-2 and TSG101 in a Ca2+-dependent manner, HD-PTP interacted with ALG-2 Ca2+-dependently but with TSG101 Ca2+-independently.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Biosciences
Publisher:	Elsevier
ISSN:	0003-9861
Last Modified:	27 Oct 2022 08:45
URI:	https://orca.cardiff.ac.uk/id/eprint/63280

Citation Data

Cited 53 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item