AP2M1: A Drug Target / Disease Biomarker (G1173)

Target Name: AP2M1

NCBI ID: G1173

AP2M1

AP2M1: A Drug Target / Disease Biomarker

AP2M1, also known as ASPERGILLUS progressus, is a type of fungus that can cause a variety of skin infections, including ringworm, athlete's foot, and toenail fungus. It is a common cause of skin infections and can be difficult to treat, particularly in cases where the infection has spread to a deeper layer of the skin.

Recent studies have suggested that AP2M1 may have potential as a drug target or biomarker for the treatment of skin infections.

One potential mechanism by which AP2M1 may be involved in the development and progression of skin infections is its ability to produce a variety of toxins and enzymes that can cause damage to the skin and disrupt the immune system. These toxins and enzymes can cause inflammation, itching, and other symptoms that can make the infection more difficult to treat.

Another potential mechanism by which AP2M1 may be involved in the development and progression of skin infections is its ability to invade and colonize the skin. Many skin infections, including ringworm and athlete's foot, require treatment with antifungal medications that can effectively disrupt the fungal colonization that can cause the infection.

In addition to its potential as a drug target or biomarker, AP2M1 may also be a useful diagnostic tool for the diagnosis of skin infections. The presence of AP2M1 in a skin biopsy can often be used to confirm a diagnosis of ringworm, athlete's foot, or other fungal infections.

Despite its potential as a drug target or biomarker, AP2M1 is still a relatively unstudied fungus that has not yet been fully optimized for medical use. Further research is needed to fully understand its potential role in the treatment of skin infections and to develop safe and effective treatments.

In conclusion, AP2M1 is a type of fungus that has the potential to be a drug target or biomarker for the treatment of skin infections. Its ability to produce toxins and enzymes that can cause damage to the skin and invade and colonize the skin make it a promising candidate for antifungal therapy. Further research is needed to fully understand its potential and to develop safe and effective treatments.

Protein Name: Adaptor Related Protein Complex 2 Subunit Mu 1

Functions: Component of the adaptor protein complex 2 (AP-2) (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis (PubMed:16581796). AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules (By similarity). AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway (PubMed:19033387). During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs (By similarity). The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at Thr-156 in membrane-associated AP-2 (PubMed:11877457). The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (PubMed:11877457). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity)

The "AP2M1 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 AP2M1 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.tech.

More Common Targets