Unlocking the Potential of APPL2: A novel Adaptor Protein Target for Drug Development

Target Name: APPL2

NCBI ID: G55198

APPL2

Other Name(s): adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 2 | DCC-interacting protein 13-beta (isoform 2) | DCC-interacting protein 13 beta | APPL2 variant 2 | DCC-interacting protein 13-beta (isoform 1) | Adapter protein containing PH domain, PTB domain and leucine zipper motif 2 | DIP13 beta | DP13B_HUMAN | Dip13-beta | DIP13B | Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 2, transcript variant 2 | Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 2, transcript variant 1 | adapter protein containing PH domain, PTB domain and leucine zipper motif 2 | APPL2 variant 1 | DCC-interacting protein 13-beta | adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 2

Unlocking the Potential of APPL2: A novel Adaptor Protein Target for Drug Development

Apoptosis, the process of natural cell death, is tightly regulated to maintain tissue homeostasis and promote tissue repair. However, when cellular stress accumulates to an extent that cannot be resolved, apoptosis becomes uncontrollable and can lead to various diseases, including cancer. The adaptor protein, PH domain, and leucine zipper 2 (APPL2) are involved in the regulation of apoptosis and have been identified as potential drug targets or biomarkers. In this article, we will explore the APPL2 protein and its potential as a drug target.

The APPL2 Protein

The APPL2 protein is a member of the adaptor protein family, which plays a critical role in protein-protein interactions and is involved in various cellular processes, including cell signaling, DNA replication, and apoptosis. The APPL2 protein was identified as a potential drug target due to its involvement in the regulation of apoptosis.

PH Domain

The PH domain is a key region of the APPL2 protein that is involved in the regulation of protein-protein interactions and is known for its ability to interact with various protein partners, including tyrosine. The PH domain is responsible for the regulation of tyrosine phosphorylation, which is a critical step in the regulation of cellular signaling pathways.

Leucine Zipper 2 (APPL2)

The APPL2 protein is also known as PH-associated protein (PAP) and is involved in the regulation of various cellular processes, including cell signaling, DNA replication, and apoptosis. The APPL2 protein is composed of a N-terminal PH domain, a catalytic center, and a C-terminal transmembrane region.

APPL2's Interaction with PH Domain

The PH domain of the APPL2 protein is involved in the regulation of tyrosine phosphorylation, which is a critical step in the regulation of cellular signaling pathways. Tyrosine phosphorylation is a modification that allows proteins to interact with other proteins and to regulate various cellular processes.

The PH domain of the APPL2 protein is known for its ability to interact with various protein partners, including tyrosine. This interaction between the PH domain and tyrosine is crucial for the regulation of cellular signaling pathways and for the proper functioning of the APPL2 protein.

APPL2's Interaction with Leucine Zipper 2 (APPL2)

The APPL2 protein is also known as PH-associated protein (PAP) and is involved in the regulation of various cellular processes, including cell signaling, DNA replication, and apoptosis. The APPL2 protein is composed of a N-terminal PH domain, a catalytic center, and a C-terminal transmembrane region.

The PH domain of the APPL2 protein is also involved in the regulation of the activity of APPL2. The PH domain of APPL2 interacts with the PH domain of the APPL2 protein, which results in the regulation of APPL2's activity. This interaction between the PH domains of APPL2 and APPL2 is crucial for the proper functioning of the APPL2 protein.

Drug Targeting

The APPL2 protein is a potential drug target due to its involvement in the regulation of apoptosis and its interaction with the PH domain and APPL2. Drugs that target the APPL2 protein have the potential to inhibit the regulation of apoptosis and prevent the development of various diseases, including cancer.

Conclusion

In conclusion, the APPL2 protein is a potential drug target due to its involvement in the regulation of apoptosis and its interaction with the PH domain and APPL2. The regulation of apoptosis is critical for maintaining tissue homeostasis and promoting tissue repair, and drugs that target the APPL2 protein have the potential to inhibit this regulation and prevent the development of various diseases. Further research is needed to fully understand the

Protein Name: Adaptor Protein, Phosphotyrosine Interacting With PH Domain And Leucine Zipper 2

Functions: Multifunctional adapter protein that binds to various membrane receptors, nuclear factors and signaling proteins to regulate many processes, such as cell proliferation, immune response, endosomal trafficking and cell metabolism (PubMed:26583432, PubMed:15016378, PubMed:24879834). Regulates signaling pathway leading to cell proliferation through interaction with RAB5A and subunits of the NuRD/MeCP1 complex (PubMed:15016378). Plays a role in immune response by modulating phagocytosis, inflammatory and innate immune responses. In macrophages, enhances Fc-gamma receptor-mediated phagocytosis through interaction with RAB31 leading to activation of PI3K/Akt signaling. In response to LPS, modulates inflammatory responses by playing a key role on the regulation of TLR4 signaling and in the nuclear translocation of RELA/NF-kappa-B p65 and the secretion of pro- and anti-inflammatory cytokines. Also functions as a negative regulator of innate immune response via inhibition of AKT1 signaling pathway by forming a complex with APPL1 and PIK3R1 (By similarity). Plays a role in endosomal trafficking of TGFBR1 from the endosomes to the nucleus (PubMed:26583432). Plays a role in cell metabolism by regulating adiponecting ans insulin signaling pathways and adaptative thermogenesis (PubMed:24879834) (By similarity). In muscle, negatively regulates adiponectin-simulated glucose uptake and fatty acid oxidation by inhibiting adiponectin signaling pathway through APPL1 sequestration thereby antagonizing APPL1 action (By similarity). In muscles, negativeliy regulates insulin-induced plasma membrane recruitment of GLUT4 and glucose uptake through interaction with TBC1D1 (PubMed:24879834). Plays a role in cold and diet-induced adaptive thermogenesis by activating ventromedial hypothalamus (VMH) neurons throught AMPK inhibition which enhances sympathetic outflow to subcutaneous white adipose tissue (sWAT), sWAT beiging and cold tolerance (By similarity). Also plays a role in other signaling pathways namely Wnt/beta-catenin, HGF and glucocorticoid receptor signaling (PubMed:19433865) (By similarity). Positive regulator of beta-catenin/TCF-dependent transcription through direct interaction with RUVBL2/reptin resulting in the relief of RUVBL2-mediated repression of beta-catenin/TCF target genes by modulating the interactions within the beta-catenin-reptin-HDAC complex (PubMed:19433865). May affect adult neurogenesis in hippocampus and olfactory system via regulating the sensitivity of glucocorticoid receptor. Required for fibroblast migration through HGF cell signaling (By similarity)

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