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ULK1 (show ULK1 Proteins)/2 function as a bifurcate-signaling node that sustains glucose metabolic fluxes besides initiation of autophagy in response to nutritional deprivation.
Knockdown of ULK2 expression significantly induced autophagy, EMT (show ITK Proteins), and cell migration in lung cancer cell line.
miR (show MLXIP Proteins)-26b was down-regulated in LNCaP, DU145, C4-2 and PC-3 (show PCSK1 Proteins) cells compared to the two normal prostate cells RWPE-1 and WPMY-1 except DU145 cells. This inversely correlates with ULK2 level in the same cell lines.
a novel signaling pathway identified whereby starvation-induced activation of ULK leads to phosphorylation of endogenous DENND3, with subsequent activation of Rab12 and initiation of membrane trafficking events required for autophagy
Kapbeta2 interacts with ULK2 through ULK2's putative PY-NLS (show ALDH1A2 Proteins) motif, and facilitates transport from the cytoplasm to the nucleus, depending on its Ser1027 residue phosphorylation by PKA, thereby reducing autophagic activity.
Glioblastoma and glioma cell lines had low levels of ULK2 transcripts. ULK2 promoter methylation and transcript levels showed significant negative correlation.
First identification and naming of ULK2 as an ortholog of mouse ULK2.
In response to DNA damage, ULK1 (show ULK1 Proteins) and ULK2 are upregulated by p53 (show TP53 Proteins). The upregulation of ULK1 (show ULK1 Proteins) (ULK2)/ATG13 (show ATG13 Proteins) complex by p53 (show TP53 Proteins) is necessary for the sustained autophagy activity induced by DNA damage.
The ULK-Atg13 (show ATG13 Proteins)-FIP200 complexes are direct targets of mTOR (show FRAP1 Proteins) and important regulators of autophagy in response to mTOR (show FRAP1 Proteins) signaling.
Regulation of endoplasmic reticulum-to-Golgi trafficking by ULK1 (show ULK1 Proteins)/2 is essential for cellular homeostasis.
autophagy can be executed by mechanisms that are dependent or independent of the ULK1 (show ULK1 Proteins)/2-ATG13 (show ATG13 Proteins) interaction.
AnxA2 (show ANXA2 Proteins) regulates autophagy, thereby contributing to host immunity against bacteria through the Akt1 (show AKT1 Proteins)-mTOR (show FRAP1 Proteins)-ULK1 (show ULK1 Proteins)/2 signaling pathway
ULK2 induced autophagy and inhibited growth in Ras-transformed immortalized Baby Mouse Kidney (iBMK) ATG5(+/+) but not in autophagy-deficient ATG5(-/-) cells.
Ulk1 (show ULK1 Proteins) knockdown reduced fatty acid oxidation and enhanced fatty acid uptake, the metabolic changes that could contribute to adipogenesis, whereas Ulk2 knockdown had opposing effects.
Analysis of the autophagy signaling pathway showed the existence of a negative feedback loop between the ULK1 (show ULK1 Proteins) and 2 and MTORC1 and 2, in lung tissue.
ULK1 (show ULK1 Proteins) and ULK2 have redundant roles in nutrient-dependent activation of autophagy
ULK1 (show ULK1 Proteins) and ULK2 are functionally redundant protein kinases required to mediate autophagy under nutrient-deprived conditions in fibroblasts.
the autophagy response to the enhanced amino acid catabolism induced by deprivation of glucose or direct exposure to ammonia does not require ULK1 (show ULK1 Proteins) and/or ULK2
Ulk2, which interacts with Kctd12 proteins via a small proline-serine rich domain, promotes branching and elaboration of dendrites
This gene encodes a protein that is similar to a serine/threonine kinase in C. elegans which is involved in axonal elongation. The structure of this protein is similar to the C. elegans protein in that both proteins have an N-terminal kinase domain, a central proline/serine rich (PS) domain, and a C-terminal (C) domain. The gene is located within the Smith-Magenis syndrome region on chromosome 17. Alternatively spliced transcript variants encoding the same protein have been identified.
unc-51-like kinase 2 (C. elegans)
, serine/threonine-protein kinase ULK2
, Unc-51 like kinase 2
, serine/threonine-protein kinase Unc51.2
, unc-51-like kinase 2