- Peptide Substrates
- Binding Proteins
- Secondary Antibodies
- Regulatory proteins
- 脂类激酶
- 双加氧酶与蛋白质
- 脂质底物
- E2
- Assay Buffer and Co-factors
- Methyltransferases
- Acetyltransferases
- Transcription Proteins
- COVID-19 ELISA Kits
- Tau Proteins
- Microtubule & Actin Associated Proteins
- Carbohydrate Substrates
- COVID-19 Proteins
- Chemokines
- 标记抗体
- 授予称号
- E3
Overview:
ULK1 is a serine/threonine protein kinase that plays critical role during initial stages of autophagy which is a vital response to nutrient starvation. The conserved C-terminal domain (CTD) of ULK1 controls the regulatory function and localization of the protein. Knockdown of ULK1 inhibits the autophagic response as well as inhibiting rapamycin-induced autophagy consistent with a role downstream of mTOR (1). ULK1 forms a complex with FIP200 and ATG13 and this complex is essential for starvation-induced autophagy (2). Both FIP200 and ATG13 are critical for correct localization of ULK1 to the pre-autophagosome and stability of ULK1 protein. ULK1 is phosphorylated by the mTOR pathway in a nutrient starvation-regulated manner.
Gene Aliases:
ATG1, UNC51, Unc51.1, FLJ38455
Genbank Number:
BC111603
References:
1. Ganley I G, et al: ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy. J Biol Chem. 2009 May 1;284(18):12297-305. 2. Chan E Y, et al: siRNA screening of the kinome identifies ULK1 as a multidomain modulator of autophagy. J Biol Chem. 2007 Aug 31;282(35):25464-74.