PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26859355-3 2016 Here we demonstrate that M phase-specific phosphorylation of the intramolecular interaction site within the proline-rich domain (PRD) of ALIX transforms cytosolic ALIX from closed to open conformation. Proline 108-115 programmed cell death 6 interacting protein Homo sapiens 137-141 34688656-3 2021 As evidenced by transmission electron microscopy and fluorescence and CD spectroscopy, the proline-rich domain (PRD) of ALIX, which encodes binding epitopes of multiple cellular partners, formed rope-like beta-sheet-rich reversible amyloid fibrils that dissolved upon Src-mediated phosphorylation and were restored on PTP1B-mediated dephosphorylation of its conserved tyrosine residues. Proline 91-98 programmed cell death 6 interacting protein Homo sapiens 120-124 32917811-0 2020 Proline-rich domain of human ALIX contains multiple TSG101-UEV interaction sites and forms phosphorylation-mediated reversible amyloids. Proline 0-7 programmed cell death 6 interacting protein Homo sapiens 29-33 32917811-2 2020 Using a "divide-and-conquer" approach, we present a detailed investigation of a PRD (166 residues; ~30% prolines) belonging to a human protein ALIX, a versatile adaptor protein involved in essential cellular processes including ESCRT-mediated membrane remodeling, cell adhesion, and apoptosis. Proline 104-112 programmed cell death 6 interacting protein Homo sapiens 143-147 30824759-6 2019 We revealed that the interaction between the SH3 domain of c-Src and the proline-rich region of Alix activates ESCRT-mediated intra-luminal vesicle (ILV) formation, resulting in the upregulation of exosome secretion in c-Src-transformed cells. Proline 73-80 programmed cell death 6 interacting protein Homo sapiens 96-100 26859355-3 2016 Here we demonstrate that M phase-specific phosphorylation of the intramolecular interaction site within the proline-rich domain (PRD) of ALIX transforms cytosolic ALIX from closed to open conformation. Proline 108-115 programmed cell death 6 interacting protein Homo sapiens 163-167 21715492-2 2011 Here, we report that the C-terminal proline-rich region (PRR) of ALIX folds back against the upstream domains and auto-inhibits V domain binding to viral late domains. Proline 36-43 programmed cell death 6 interacting protein Homo sapiens 65-69 22641034-4 2012 We demonstrate that Hck SH3 recognizes an extended linear proline-rich region of Alix. Proline 58-65 programmed cell death 6 interacting protein Homo sapiens 81-85 24996823-9 2014 We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Proline 71-78 programmed cell death 6 interacting protein Homo sapiens 94-98 20670214-6 2010 Through biophysical experiments, we then identified the PRR (proline-rich region) motif of Alix that binds Hck-SH3 and determined a dissociation constant of 34.5 muM. Proline 61-68 programmed cell death 6 interacting protein Homo sapiens 91-95 20929444-4 2010 Our results demonstrate that an intramolecular interaction between Patch 2 in the Bro1 domain and the TSG101 (tumour susceptibility gene 101 protein)-docking site in the proline-rich domain locks ALIX into a closed conformation that renders ALIX unable to interact with CHMP4 and retroviral Gag proteins. Proline 170-177 programmed cell death 6 interacting protein Homo sapiens 196-200 20929444-4 2010 Our results demonstrate that an intramolecular interaction between Patch 2 in the Bro1 domain and the TSG101 (tumour susceptibility gene 101 protein)-docking site in the proline-rich domain locks ALIX into a closed conformation that renders ALIX unable to interact with CHMP4 and retroviral Gag proteins. Proline 170-177 programmed cell death 6 interacting protein Homo sapiens 241-245 19143627-2 2009 Specifically, the PTAP (Pro-Thr-Ala-Pro)-type primary L domain of HIV-1 recruits ESCRT-I by binding to Tsg101 (tumour susceptibility gene 101), and an auxiliary LYPX(n)L (Leu-Tyr-Pro-Xaa(n)-Leu)-type L domain recruits the ESCRT-III-binding partner Alix [ALG-2 (apoptosis-linked gene 2)-interacting protein X]. Proline 24-27 programmed cell death 6 interacting protein Homo sapiens 248-252 19523902-3 2009 Structural modeling based on small angle X-ray scattering (SAXS) data reveals an elongated crescent-shaped conformation for dimeric ALIX lacking the proline-rich domain (ALIX(BRO1-V)). Proline 149-156 programmed cell death 6 interacting protein Homo sapiens 132-136 19143627-2 2009 Specifically, the PTAP (Pro-Thr-Ala-Pro)-type primary L domain of HIV-1 recruits ESCRT-I by binding to Tsg101 (tumour susceptibility gene 101), and an auxiliary LYPX(n)L (Leu-Tyr-Pro-Xaa(n)-Leu)-type L domain recruits the ESCRT-III-binding partner Alix [ALG-2 (apoptosis-linked gene 2)-interacting protein X]. Proline 36-39 programmed cell death 6 interacting protein Homo sapiens 248-252 17428861-7 2007 The ability of ALIX to rescue a PTAP mutant also depends on its C-terminal proline-rich domain (PRD), but not on the binding sites for Tsg101, endophilin, CIN85, or for the newly identified binding partner, CMS, within the PRD. Proline 75-82 programmed cell death 6 interacting protein Homo sapiens 15-19 18477395-3 2008 Intriguingly, the deletion of the C-terminal proline-rich region of ALIX prevented detectable binding to p6. Proline 45-52 programmed cell death 6 interacting protein Homo sapiens 68-72 18477395-4 2008 In contrast, a four-amino acid deletion in the central hinge region of p6 increased its association with ALIX as shown by its ability to bind to ALIX lacking the proline rich domain. Proline 162-169 programmed cell death 6 interacting protein Homo sapiens 105-109 18477395-7 2008 Altogether, our data support a model where the C-terminal proline-rich domain of ALIX allows the access of its binding site to p6 by alleviating a conformational constraint resulting from the presence of the central p6 hinge. Proline 58-65 programmed cell death 6 interacting protein Homo sapiens 81-85 12860994-1 2003 Alix (ALG-2-interacting protein X) is a 95-kDa protein that interacts with an EF-hand type Ca(2+)-binding protein, ALG-2 (apoptosis-linked gene 2), through its C-terminal proline-rich region. Proline 171-178 programmed cell death 6 interacting protein Homo sapiens 0-4 16868030-5 2006 The diversity of Alix functions is due to its proline-rich C-terminus, which provides multiple protein-binding sites. Proline 46-53 programmed cell death 6 interacting protein Homo sapiens 17-21 15557335-4 2005 A proline-rich region in the C terminus of Alix bound the Src SH3 domain, but this interaction was dependent on the release of the Src SH2 domain from its Src internal ligand either by interaction with Alix Tyr319 or by mutation of Src Tyr527. Proline 2-9 programmed cell death 6 interacting protein Homo sapiens 43-47 14999017-3 2004 The region corresponding to amino acid residues 794 to 827 in the carboxy-terminal proline-rich region of Alix was sufficient to confer the ability to interact directly with ALG-2. Proline 83-90 programmed cell death 6 interacting protein Homo sapiens 106-110 16978157-1 2007 The mammalian adaptor protein Alix [ALG-2 (apoptosis-linked-gene-2 product)-interacting protein X] belongs to a conserved family of proteins that have in common an N-terminal Bro1 domain and a C-terminal PRD (proline-rich domain), both of which mediate partner protein interactions. Proline 209-216 programmed cell death 6 interacting protein Homo sapiens 30-34 17174262-0 2007 HD-PTP and Alix share some membrane-traffic related proteins that interact with their Bro1 domains or proline-rich regions. Proline 102-109 programmed cell death 6 interacting protein Homo sapiens 11-15 17174262-2 2007 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. Proline 123-130 programmed cell death 6 interacting protein Homo sapiens 23-27 16966331-4 2006 In cell-free systems, Alix directly interacts with F-actin at both the N-terminal Bro1 domain and the C-terminal proline-rich domain. Proline 113-120 programmed cell death 6 interacting protein Homo sapiens 22-26 12860994-1 2003 Alix (ALG-2-interacting protein X) is a 95-kDa protein that interacts with an EF-hand type Ca(2+)-binding protein, ALG-2 (apoptosis-linked gene 2), through its C-terminal proline-rich region. Proline 171-178 programmed cell death 6 interacting protein Homo sapiens 6-33 12445460-4 2002 Both the N-terminal regulatory domain of annexin XI (Anx11N) and the ALG-2-binding domain of Alix/AIP1 are rich in Pro, Gly, Ala, Tyr and Gln. Proline 115-118 programmed cell death 6 interacting protein Homo sapiens 93-97 12588984-4 2003 We show that both PalA and AIP1/Alix recognize a protein-protein binding motif that we denote YPXL/I, where Tyr, Pro, and Leu/Ile are crucial for its interactive properties. Proline 113-116 programmed cell death 6 interacting protein Homo sapiens 27-31 12588984-4 2003 We show that both PalA and AIP1/Alix recognize a protein-protein binding motif that we denote YPXL/I, where Tyr, Pro, and Leu/Ile are crucial for its interactive properties. Proline 113-116 programmed cell death 6 interacting protein Homo sapiens 32-36 12445460-4 2002 Both the N-terminal regulatory domain of annexin XI (Anx11N) and the ALG-2-binding domain of Alix/AIP1 are rich in Pro, Gly, Ala, Tyr and Gln. Proline 115-118 programmed cell death 6 interacting protein Homo sapiens 98-102