PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17295840-7 2007 This analysis suggests that Atg17p is the most basic protein in PAS organization: when it is specifically targeted to the plasma membrane, other Atg proteins are recruited to that location, suggesting that Atg17p acts as a scaffold protein to organize Atg proteins to the PAS. Aminosalicylic Acid 64-67 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 28-34 29321961-2 2018 In budding yeast, autophagosomes are generated from the preautophagosomal structure (PAS), in which Atg11 and Atg17 function as scaffolds essential for selective and nonselective types of autophagy, respectively. Aminosalicylic Acid 85-88 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 110-115 27404361-1 2016 Autophagosome formation in yeast entails starvation-induced assembly of the pre-autophagosomal structure (PAS), in which multiple Atg1 complexes (composed of Atg1, Atg13, and the Atg17-Atg29-Atg31 subcomplex) are initially engaged. Aminosalicylic Acid 106-109 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 179-184 26986547-5 2016 We recently showed that 2 autophagy scaffold proteins, the Atg17-Atg31-Atg29 complex and Atg11, regulate autophagosome-vacuole fusion by recruiting the vacuolar SNARE Vam7 to the phagophore assembly site (PAS), where an autophagosome forms in yeast. Aminosalicylic Acid 205-208 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 59-64 25773276-4 2015 The Atg17-Atg31-Atg29 complex forms a scaffold for PAS organization, and recruits other autophagy-related (Atg) proteins to the PAS. Aminosalicylic Acid 51-54 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 4-9 25773276-4 2015 The Atg17-Atg31-Atg29 complex forms a scaffold for PAS organization, and recruits other autophagy-related (Atg) proteins to the PAS. Aminosalicylic Acid 128-131 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 4-9 18298591-10 2008 In conditions inducing autophagy, Irs4p and Tax4p partially localized to the pre-autophagosomal structure (PAS) and are required to efficiently recruit to the PAS Atg17p, a factor modulating the autophagic response. Aminosalicylic Acid 107-110 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 163-169 18298591-10 2008 In conditions inducing autophagy, Irs4p and Tax4p partially localized to the pre-autophagosomal structure (PAS) and are required to efficiently recruit to the PAS Atg17p, a factor modulating the autophagic response. Aminosalicylic Acid 159-162 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 163-169 18077553-8 2008 The Atg1 C terminus mediates an interaction with Atg13 and Atg17, facilitating a structural role of Atg1 that is needed to efficiently organize an initial step of PAS assembly, whereas Atg1 kinase activity affects the dynamics of protein movement at the PAS involved in Atg protein cycling. Aminosalicylic Acid 163-166 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 59-64 18077553-8 2008 The Atg1 C terminus mediates an interaction with Atg13 and Atg17, facilitating a structural role of Atg1 that is needed to efficiently organize an initial step of PAS assembly, whereas Atg1 kinase activity affects the dynamics of protein movement at the PAS involved in Atg protein cycling. Aminosalicylic Acid 254-257 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 59-64 29065154-5 2017 In particular, the S-shaped Atg17-Atg31-Atg29 subcomplex of Atg1 is critical for phagophore nucleation at the PAS. Aminosalicylic Acid 110-113 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 28-33 29065154-10 2017 Our finding rationalizes the recruitment of Atg17 complexes to the yeast PAS, and their unusual shape. Aminosalicylic Acid 73-76 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 44-49 24793651-2 2014 Starvation-induced dephosphorylation of Atg13 is required for the formation of the Atg1-Atg13-Atg17-Atg29-Atg31 complex (Atg1 complex), a prerequisite for PAS assembly. Aminosalicylic Acid 155-158 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 94-99 23549786-6 2013 The PAS scaffold proteins (Atg13 and Atg17) and phosphatidylinositol 3-kinase complex I were localized to a position at the junction between the IM and the vacuolar membrane, termed the vacuole-IM contact site (VICS). Aminosalicylic Acid 4-7 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 37-42 23219485-3 2012 The crystal structure of a 2:2:2 complex of the earliest acting PAS proteins, Atg17, Atg29, and Atg31, was solved at 3.05 A resolution. Aminosalicylic Acid 64-67 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 78-83 23219485-5 2012 Dimerization of the Atg17-Atg31-Atg29 complex is critical for both PAS formation and autophagy, and each dimer contains two separate and complete crescents. Aminosalicylic Acid 67-70 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 20-25 19371383-5 2009 Here, we demonstrate that, in autophagy-inducing condition, Atg9 is recruited to the PAS in a manner dependent on Atg17. Aminosalicylic Acid 85-88 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 114-119 19371383-8 2009 Consistently, the Atg17-dependent PAS localization of Atg9 requires Atg1. Aminosalicylic Acid 34-37 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 18-23 18552550-5 2008 We found that Atg1, Atg13 and Atg17 play a similar role for PAS formation under autophagy-inducing conditions as seen for Atg11 during vegetative growth. Aminosalicylic Acid 60-63 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 30-35 18552550-7 2008 Atg1 plays a structural role for efficient recruitment of Atg proteins to the PAS, which is mediated by interaction with Atg13 and Atg17. Aminosalicylic Acid 78-81 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 131-136 17295840-7 2007 This analysis suggests that Atg17p is the most basic protein in PAS organization: when it is specifically targeted to the plasma membrane, other Atg proteins are recruited to that location, suggesting that Atg17p acts as a scaffold protein to organize Atg proteins to the PAS. Aminosalicylic Acid 64-67 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 206-212 17295840-7 2007 This analysis suggests that Atg17p is the most basic protein in PAS organization: when it is specifically targeted to the plasma membrane, other Atg proteins are recruited to that location, suggesting that Atg17p acts as a scaffold protein to organize Atg proteins to the PAS. Aminosalicylic Acid 272-275 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 28-34 17295840-7 2007 This analysis suggests that Atg17p is the most basic protein in PAS organization: when it is specifically targeted to the plasma membrane, other Atg proteins are recruited to that location, suggesting that Atg17p acts as a scaffold protein to organize Atg proteins to the PAS. Aminosalicylic Acid 272-275 protein kinase regulatory subunit ATG17 Saccharomyces cerevisiae S288C 206-212