ATG17/YLR423C Summary Help

Standard Name ATG17 1
Systematic Name YLR423C
Alias APG17 2
Feature Type ORF, Verified
Description Scaffold protein responsible for phagophore assembly site organization; regulatory subunit of an autophagy-specific complex that includes Atg1p and Atg13p; stimulates Atg1p kinase activity; human ortholog RB1CC1/FIP200 interacts with p53, which inhibits autophagy in human cells (3, 4, 5, 6, 7 and see Summary Paragraph)
Name Description AuTophaGy related 1
Chromosomal Location
ChrXII:973170 to 971917 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All ATG17 GO evidence and references
  View Computational GO annotations for ATG17
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 1 genes
Resources
Classical genetics
null
overexpression
Large-scale survey
null
Resources
232 total interaction(s) for 159 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 19
  • Affinity Capture-Western: 20
  • Co-purification: 2
  • Two-hybrid: 138

Genetic Interactions
  • Negative Genetic: 30
  • Phenotypic Enhancement: 3
  • Positive Genetic: 13
  • Synthetic Growth Defect: 4
  • Synthetic Lethality: 3

Resources
Expression Summary
histogram
Resources
Length (a.a.) 417
Molecular Weight (Da) 48,656
Isoelectric Point (pI) 4.8
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXII:973170 to 971917 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1254 973170..971917 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004415
SUMMARY PARAGRAPH for ATG17

about autophagy...

Autophagy is a highly conserved eukaryotic pathway for sequestering and transporting bulk cytoplasm, including proteins and organelle material, to the lysosome for degradation (reviewed in 8). Upon starvation for nutrients such as carbon, nitrogen, sulfur, and various amino acids, or upon endoplasmic reticulum stress, cells initiate formation of a double-membrane vesicle, termed an autophagosome, that mediates this process (9, 10, reviewed in 11). Approximately 30 autophagy-related (Atg) proteins have been identified in S. cerevisiae, 17 of which are essential for formation of the autophagosome (reviewed in 12). Null mutations in most of these genes prevent induction of autophagy, and cells do not survive nutrient starvation; however, these mutants are viable in rich medium. Some of the Atg proteins are also involved in a constitutive biosynthetic process termed the cytoplasm-to-vacuole targeting (Cvt) pathway, which uses autophagosomal-like vesicles for selective transport of hydrolases aminopeptidase I (Lap4p) and alpha-mannosidase (Ams1p) to the vacuole (13, 14).

Autophagy proceeds via a multistep pathway (a summary diagram (download pdf) kindly provided by Dan Klionsky). First, nutrient availability is sensed by the TORC1 complex and also cooperatively by protein kinase A and Sch9p (15, 16). Second, signals generated by the sensors are transmitted to the autophagosome-generating machinery comprised of the 17 Atg gene products. These 17 proteins collectively form the pre-autophagosomal structure/phagophore assembly site (PAS). The PAS generates an isolation membrane (IM), which expands and eventually fuses along the edges to complete autophagosome formation. At the vacuole the outer membrane of the autophagosome fuses with the vacuolar membrane and autophagic bodies are released, disintegrated, and their contents degraded for reuse in biosynthesis (17 and reviewed in 12).

about ATG17

Atg17p is an autophagy-specific protein that acts as a scaffold for the other ATG proteins during PAS organization (6, 18). Atg17p has many interaction partners and may form complexes with proteins such as Atg20p, Snx4p, Atg29p, Cis1p, and Atg11p to localize other factors to the PAS (19, 18, 14). Efficient localization of Atg17p to the PAS is itself dependent on the EPS15 homology domain proteins Irs4p and Tax4p (20).

Atg17p, along with Atg13p, is also a regulatory subunit of the Atg1p protein kinase complex and is required for vesicle expansion during autophagy (5, 4, reviewed in 12). Atg13p and Atg17p stimulate Atg1p kinase activity and formation of this complex is specific to autophagy and enhanced during starvation (4).

atg17 mutants are defective in autophagy, blocked in pexophagy, have lengthened telomeres, and cannot survive under starvation conditions (5, 21, 4). Autophagosomes in atg17 null mutants are fewer in number and less than half the normal size (5, 4). Overexpression of ATG17 inhibits filamentous growth (22). ATG17 homologs have been identified in all yeast species and most filamentous fungi studied to date, but no ATG17 ortholog has yet been identified in higher eukaryotes (23).

about autophagy nomenclature

The initial identification of factors involved in autophagy was carried out by several independent labs, which led to a proliferation of nomenclature for the genes and gene products involved. The differing gene name acronyms from these groups included APG, AUT, CVT, GSA, PAG, PAZ, and PDD (1 and references therein). A concerted effort was made in 2003 by the scientists working in the field to unify the nomenclature for these genes, and "AuTophaGy-related" genes are now denoted by the letters ATG (1). In addition to the ATG gene names that have been assigned to S. cerevisiae proteins and their orthologs, several ATG gene names, including ATG25, ATG28, and ATG30, have been used to designate proteins in other ascomycete yeast species for which there is no identifiable equivalent in S. cerevisiae (23, 24).

Last updated: 2008-02-08 Contact SGD

References cited on this page View Complete Literature Guide for ATG17
1) Klionsky DJ, et al.  (2003) A unified nomenclature for yeast autophagy-related genes. Dev Cell 5(4):539-45
2) Kamada Y, et al.  (2000) Tor-mediated induction of autophagy via an Apg1 protein kinase complex. J Cell Biol 150(6):1507-13
3) Tsukada M and Ohsumi Y  (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett 333(1-2):169-74
4) Kabeya Y, et al.  (2005) Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy. Mol Biol Cell 16(5):2544-53
5) Cheong H, et al.  (2005) Atg17 regulates the magnitude of the autophagic response. Mol Biol Cell 16(7):3438-53
6) Suzuki K, et al.  (2007) Hierarchy of Atg proteins in pre-autophagosomal structure organization. Genes Cells 12(2):209-18
7) Morselli E, et al.  (2011) p53 inhibits autophagy by interacting with the human ortholog of yeast Atg17, RB1CC1/FIP200. Cell Cycle 10(16):2763-9
8) Budovskaya YV, et al.  (2004) The Ras/cAMP-dependent protein kinase signaling pathway regulates an early step of the autophagy process in Saccharomyces cerevisiae. J Biol Chem 279(20):20663-71
9) Takeshige K, et al.  (1992) Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction. J Cell Biol 119(2):301-11
10) Matsuura A, et al.  (1997) Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae. Gene 192(2):245-50
11) Yorimitsu T and Klionsky DJ  (2007) Endoplasmic reticulum stress: a new pathway to induce autophagy. Autophagy 3(2):160-2
12) Suzuki K and Ohsumi Y  (2007) Molecular machinery of autophagosome formation in yeast, Saccharomyces cerevisiae. FEBS Lett 581(11):2156-61
13) Harding TM, et al.  (1996) Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway. J Biol Chem 271(30):17621-4
14) Yorimitsu T and Klionsky DJ  (2005) Atg11 links cargo to the vesicle-forming machinery in the cytoplasm to vacuole targeting pathway. Mol Biol Cell 16(4):1593-605
15) Yorimitsu T, et al.  (2007) Protein Kinase A and Sch9 Cooperatively Regulate Induction of Autophagy in Saccharomyces cerevisiae. Mol Biol Cell 18(10):4180-9
16) Noda T and Ohsumi Y  (1998) Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J Biol Chem 273(7):3963-6
17) Suzuki K, et al.  (2001) The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation. EMBO J 20(21):5971-81
18) Kawamata T, et al.  (2008) Organization of the Pre-autophagosomal Structure Responsible for Autophagosome Formation. Mol Biol Cell 19(5):2039-50
19) Nice DC, et al.  (2002) Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagy. J Biol Chem 277(33):30198-207
20) Bugnicourt A, et al.  (2008) Irs4p and Tax4p: two redundant EH domain proteins involved in autophagy. Traffic 9(5):755-69
21) Gatbonton T, et al.  (2006) Telomere length as a quantitative trait: genome-wide survey and genetic mapping of telomere length-control genes in yeast. PLoS Genet 2(3):e35
22) Ma J, et al.  (2007) Overexpression of autophagy-related genes inhibits yeast filamentous growth. Autophagy 3(6):604-9
23) Meijer WH, et al.  (2007) ATG genes involved in non-selective autophagy are conserved from yeast to man, but the selective Cvt and pexophagy pathways also require organism-specific genes. Autophagy 3(2):106-16
24) Farre JC, et al.  (2008) PpAtg30 tags peroxisomes for turnover by selective autophagy. Dev Cell 14(3):365-76