What does ATF 6 do?

What does ATF 6 do?

ATF6 is an endoplasmic reticulum (ER) stress-regulated transmembrane transcription factor that activates the transcription of ER molecules. Accumulation of misfolded proteins in the Endoplasmic Reticulum results in the proteolytic cleavage of ATF6.

What does ATF6 do in the UPR?

Upon activation of UPR, ATF6 is released and displays a Golgi localization sequence. ATF6α disulfide bounds are also remodeled upon ER stress, which allows the molecule to be translocated to the Golgi apparatus. In the latter compartment, it is cleaved by the Site-1 and Site-2 protease (S1P and S2P).

Is chop a protein?

CHOP belongs to the family of CCAAT/enhancer binding proteins (C/EBPs) and is involved in the regulation of genes that encode proteins involved in proliferation, differentiation and expression, and energy metabolism. CHOP is a 29 kD protein with 169 (human) or 168 (rodents) amino acid residues.

How does BiP protein work?

BiP is a HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum (ER) that binds newly synthesized proteins as they are translocated into the ER, and maintains them in a state competent for subsequent folding and oligomerization.

What happens if endoplasmic reticulum fails?

The impairment of the canonical UPR/ER stress downstream pathway has been termed ‘ER stress response failure’, which ultimately reduces cell survival and induces cell death, leading to disease progression.

What activates ATF3?

for example, found that ATF3 is induced by proinflammatory cytokines, glucose, and palmitate in ß cells (25). ATF3 induction is partially mediated by the NF-κB and JNK/stress-activated protein kinase (SAPK) signaling pathways, which are two stress-induced pathways involved in diabetes.

What is Batf3?

Basic leucine zipper transcription factor ATF-like 3 (Batf3) is a member of the AP-1 transcription factor family. Batf3 binds to DNA along with c-Jun and nuclear factor of activated T cells (NFAT), thereby competing with c-Fos to form a heterodimer with c-Jun.

What is the difference between a chaperone and a chaperonin?

Chaperones refer to the proteins which assist the covalent folding or unfolding and assembly and disassembly of other macromolecular structures while chaperonins refer to the proteins which provide favorable conditions for the correct folding of denatured proteins, preventing aggregation.

What is a client protein?

A term of art for a protein which is manipulated or processed, as in the folding of a client protein by a chaperone.

Where is BiP located?

lumen of the endoplasmic reticulum (ER)
BiP, an HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum (ER), binds newly-synthesized proteins as they are translocated into the ER and maintains them in a state competent for subsequent folding and oligomerization.

What diseases can the ER cause?

There is accumulating evidence implicating prolonged ER stress in the development and progression of many diseases, including neurodegeneration, atherosclerosis, type 2 diabetes, liver disease, and cancer.