SORL1: A Promising Drug Target and Biomarker for Proteostasis

Target Name: SORL1

NCBI ID: G6653

SORL1

SORL1: A Promising Drug Target and Biomarker for Proteostasis

S Sorting protein-related receptor containing LDLR class A repeats (SORL1) is a protein that plays a crucial role in the regulation of intracellular signaling pathways, including the T cell receptor (TCR) signaling pathway. The SORL1 receptor is a member of the T cell receptor superfamily and is expressed in various tissues, including the brain, pancreas, and gastrointestinal tract. SORL1 has been implicated in the development and progression of several diseases, including autoimmune diseases, cancer, and neurodegenerative diseases.

SORL1 Receptor Signaling

SORL1 is a transmembrane protein that consists of an extracellular domain, a transmembrane domain, and an intracellular domain. The extracellular domain is involved in SORL1's ability to interact with ligands, while the transmembrane domain is responsible for the receptor's overall structure and function. The intracellular domain is responsible for the SORL1 receptor's ability to interact with intracellular signaling molecules, including the protein kinase A (PKA).

SORL1 has been shown to play a role in the regulation of intracellular signaling pathways, including the T cell receptor (TCR) signaling pathway. The SORL1 receptor is a critical regulator of T cell development and function, as it is involved in the negative regulation of T cell proliferation and the regulation of T cell antigen presentation.

SORL1 has been shown to play a role in the regulation of the T cell receptor (TCR) signaling pathway. The SORL1 receptor is a critical regulator of T cell development and function, as it is involved in the negative regulation of T cell proliferation and the regulation of T cell antigen presentation.

SORL1 has been shown to play a role in the regulation of the DNA damage response (DDR) pathway. The SORL1 receptor is involved in the regulation of DNA double-strand break repair, as well as the regulation of cell apoptosis.

Mutations in SORL1

Mutations in SORL1 have been implicated in the development and progression of several diseases, including autoimmune diseases, cancer, and neurodegenerative diseases. SORL1 mutations have been shown to alter the SORL1 receptor's structure and function, leading to the disruption of its normal function.

SORL1 Mutations and Disease

SORL1 mutations have been shown to alter the SORL1 receptor's structure and function, leading to the disruption of its normal function. SORL1 mutations have been implicated in the development and progression of several diseases, including autoimmune diseases, cancer, and neurodegenerative diseases.

SORL1 has been shown to play a role in the development and progression of autoimmune diseases, such as rheumatoid arthritis (RA) and multiple sclerosis (MS). SORL1 mutations have been shown to alter the SORL1 receptor's function, leading to the disruption of its ability to regulate T cell development and function.

SORL1 has also been shown to be involved in the development and progression of cancer, including colon cancer. SORL1 mutations have been shown to alter the SORL1 receptor's function, leading to the disruption of its ability to regulate cell apoptosis.

SORL1 has also been shown to be involved in the development and progression of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. SORL1 mutations have been shown to alter the SORL1 receptor's function, leading to the disruption of its ability to regulate

Protein Name: Sortilin Related Receptor 1

Functions: Sorting receptor that directs several proteins to their correct location within the cell (Probable). Along with AP-1 complex, involved Golgi apparatus - endosome sorting (PubMed:17646382). Sorting receptor for APP, regulating its intracellular trafficking and processing into amyloidogenic-beta peptides. Retains APP in the trans-Golgi network, hence preventing its transit through late endosomes where amyloid beta peptides Abeta40 and Abeta42 are generated (PubMed:16174740, PubMed:16407538, PubMed:17855360, PubMed:24523320). May also sort newly produced amyloid-beta peptides to lysosomes for catabolism (PubMed:24523320). Does not affect APP trafficking from the endoplasmic reticulum to Golgi compartments (PubMed:17855360). Sorting receptor for the BDNF receptor NTRK2/TRKB that facilitates NTRK2 trafficking between synaptic plasma membranes, postsynaptic densities and cell soma, hence positively regulates BDNF signaling by controlling the intracellular location of its receptor (PubMed:23977241). Sorting receptor for GDNF that promotes GDNF regulated, but not constitutive secretion (PubMed:21994944). Sorting receptor for the GDNF-GFRA1 complex, directing it from the cell surface to endosomes. GDNF is then targeted to lysosomes and degraded, while its receptor GFRA1 recycles back to the cell membrane, resulting in a GDNF clearance pathway. The SORL1-GFRA1 complex further targets RET for endocytosis, but not for degradation, affecting GDNF-induced neurotrophic activities (PubMed:23333276). Sorting receptor for ERBB2/HER2. Regulates ERBB2 subcellular distribution by promoting its recycling after internalization from endosomes back to the plasma membrane, hence stimulating phosphoinositide 3-kinase (PI3K)-dependent ERBB2 signaling. In ERBB2-dependent cancer cells, promotes cell proliferation (PubMed:31138794). Sorting receptor for lipoprotein lipase LPL. Promotes LPL localization to endosomes and later to the lysosomes, leading to degradation of newly synthesized LPL (PubMed:21385844). Potential sorting receptor for APOA5, inducing APOA5 internalization to early endosomes, then to late endosomes, wherefrom a portion is sent to lysosomes and degradation, another portion is sorted to the trans-Golgi network (PubMed:18603531). Sorting receptor for the insulin receptor INSR. Promotes recycling of internalized INSR via the Golgi apparatus back to the cell surface, thereby preventing lysosomal INSR catabolism, increasing INSR cell surface expression and strengthening insulin signal reception in adipose tissue. Does not affect INSR internalization (PubMed:27322061). Plays a role in renal ion homeostasis, controlling the phospho-regulation of SLC12A1/NKCC2 by STK39/SPAK kinase and PPP3CB/calcineurin A beta phosphatase, possibly through intracellular sorting of STK39 and PPP3CB (By similarity). Stimulates, via the N-terminal ectodomain, the proliferation and migration of smooth muscle cells, possibly by increasing cell surface expression of the urokinase receptor uPAR/PLAUR. This may promote extracellular matrix proteolysis and hence facilitate cell migration (PubMed:14764453). By acting on the migration of intimal smooth muscle cells, may accelerate intimal thickening following vascular injury (PubMed:14764453). Promotes adhesion of monocytes (PubMed:23486467). Stimulates proliferation and migration of monocytes/macrophages (By similarity). Through its action on intimal smooth muscle cells and macrophages, may accelerate intimal thickening and macrophage foam cell formation in the process of atherosclerosis (By similarity). Regulates hypoxia-enhanced adhesion of hematopoietic stem and progenitor cells to the bone marrow stromal cells via a PLAUR-mediated pathway. This function is mediated by the N-terminal ectodomain (PubMed:23486467). Metabolic regulator, which functions to maintain the adequate balance between lipid storage and oxidation in response to changing environmental conditions, such as temperature and diet. The N-terminal ectodomain negatively regulates adipose tissue energy expenditure, acting through the inhibition the BMP/Smad pathway (By similarity). May regulate signaling by the heterodimeric neurotrophic cytokine CLCF1-CRLF1 bound to the CNTFR receptor by promoting the endocytosis of the tripartite complex CLCF1-CRLF1-CNTFR and lysosomal degradation (PubMed:26858303). May regulate IL6 signaling, decreasing cis signaling, possibly by interfering with IL6-binding to membrane-bound IL6R, while up-regulating trans signaling via soluble IL6R (PubMed:28265003)

The "SORL1 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 SORL1 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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