Target Name: ATG4B
NCBI ID: G23192
Review Report on ATG4B Target / Biomarker Content of Review Report on ATG4B Target / Biomarker
ATG4B
Other Name(s): hAPG4B | APG4B | Autophagy related 4B cysteine peptidase, transcript variant 1 | APG4 autophagy 4 homolog B | autophagy related 4B cysteine peptidase | Cysteine protease ATG4B | ATG4B variant 1 | Cysteine protease ATG4B (isoform a) | autophagy-related protein 4 homolog B | MGC1353 | autophagin-1 | HsAPG4B | ATG4 autophagy related 4 homolog B | AUT-like 1 cysteine endopeptidase | Autophagy-related cysteine endopeptidase 1 | AUTL1 | ATG4B_HUMAN | Autophagin-1 | autophagy-related cysteine endopeptidase 1 | Autophagy-related protein 4 homolog B

ATG4B: A Potential Drug Target for Blood-Brain Barrier Development

ATG4B, also known as hAPG4B, is a gene that encodes a protein involved in the development and maintenance of the blood-brain barrier. The blood-brain barrier is a specialized barrier that separates the brain from the bloodstream, and it plays a crucial role in maintaining the health and function of the brain.

ATG4B is a member of the Atypical Glycoside Gene 4 (AGG) family, which is known for producing a wide range of unique sugars that are involved in various cellular processes. The AGG family has been identified as a potential drug target for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

ATG4B has been shown to be involved in the development and maintenance of the blood-brain barrier, which is a critical barrier that helps to protect the brain from harmful substances and substances that could cause damage. The blood-brain barrier is composed of various cell types, including endothelial cells, which line the blood vessels of the brain, and glial cells, which support and protect nerve cells.

ATG4B is involved in the development and maintenance of the blood-brain barrier by producing a variety of sugars that are essential for the structure and function of this barrier. For example, one of the sugars produced by ATG4B is called N-acetylglucoside (NAG), which is a key component of the blood-brain barrier. NAG helps to maintain the integrity of the blood-brain barrier by providing it with a sugar source that is essential for its structure and function.

In addition to its role in the blood-brain barrier, ATG4B has also been shown to be involved in various cellular processes that are important for the development and maintenance of the brain. For example, ATG4B has been shown to be involved in the production of myelin sheath, which is the protein that helps to insulate and protect nerve cells. Additionally, ATG4B has been shown to be involved in the production of neurotransmitters, which are chemical messengers that help to communicate between nerve cells.

Given its involvement in the development and maintenance of the blood-brain barrier, ATG4B is a potential drug target for various diseases. For example, it is thought to be involved in the development of neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and Huntington's disease. Additionally, ATG4B is also thought to be involved in the development of certain autoimmune disorders, such as multiple sclerosis and rheumatoid arthritis.

In conclusion, ATG4B is a gene that encodes a protein involved in the development and maintenance of the blood-brain barrier. It is a potential drug target for various diseases, including neurodegenerative diseases and autoimmune disorders. Further research is needed to fully understand the role of ATG4B in these diseases and to develop effective treatments.

Protein Name: Autophagy Related 4B Cysteine Peptidase

Functions: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:26378241, PubMed:29232556, PubMed:28821708, PubMed:30443548, PubMed:30661429, PubMed:22302004, PubMed:27527864, PubMed:28633005, PubMed:30076329). Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy (PubMed:33773106, PubMed:33909989). The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:20818167, PubMed:19322194, PubMed:21177865, PubMed:22302004, PubMed:27527864, PubMed:28633005, PubMed:29458288, PubMed:30661429, PubMed:28287329). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:22302004). Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3 (PubMed:31315929, PubMed:33773106). In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed:15187094, PubMed:28633005, PubMed:29458288, PubMed:32686895, PubMed:33909989, PubMed:19322194). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed:15187094, PubMed:29458288, PubMed:32686895, PubMed:33909989, PubMed:19322194). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989). Compared to other members of the family (ATG4A, ATG4C or ATG4C), constitutes the major protein for proteolytic activation of ATG8 proteins, while it displays weaker delipidation activity than other ATG4 paralogs (PubMed:29458288, PubMed:30661429). Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (PubMed:33773106)

The "ATG4B Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about ATG4B comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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