Member database | Pfam |
Pfam type | domain |
Short name | ATG1-like_MIT2 |
Clan | MIT |
Author | Assefa S;0000-0003-2178-533X Coggill P;0000-0001-5731-1588 Bateman A;0000-0002-6982-4660 Chuguransky S;0000-0002-0520-0736 |
Sequence Ontology | 0000417 |
Description
Members of this entry are serine/threonine-protein kinases and includes Atg1 from yeasts, Unc-51 from C. elegans and ULK1-2 from humans. Atg1 is required for vesicle formation in autophagy and the cytoplasm-to-vacuole targeting (Cvt) pathway
[2, 3]. Unc-51 is important for axonal elongation and axonal guidance
[1] and ULK1-2 are involved in autophagy in response to starvation
[4]. They consist of a kinase domain at the N-terminal (Pfam:PF00069) and two tandem microtubule interacting and transport (MIT) domains (tMIT) at the C-terminal which, in ATG1, mediates the interaction with ATG13
[2]. In ULK1-2, MIT domain control the regulatory function and localization of the proteins and also mediate interactions with additional autophagy proteins
[4]. This is the C-terminal MIT domain (MIT2).
References
1.The autophagy-related kinase UNC-51 and its binding partner UNC-14 regulate the subcellular localization of the Netrin receptor UNC-5 in Caenorhabditis elegans. Ogura K, Goshima Y. Development 133, 3441-50, (2006). View articlePMID: 16887826
2.Structural basis of starvation-induced assembly of the autophagy initiation complex. Fujioka Y, Suzuki SW, Yamamoto H, Kondo-Kakuta C, Kimura Y, Hirano H, Akada R, Inagaki F, Ohsumi Y, Noda NN. Nat Struct Mol Biol 21, 513-21, (2014). PMID: 24793651