DAPP1

Official Full Name

dual adaptor of phosphotyrosine and 3-phosphoinositides 1

Organism

Homo sapiens

GeneID

27071

Background

Enables phosphatidylinositol-3,4,5-trisphosphate binding activity and phosphatidylinositol-3,4-bisphosphate binding activity. Predicted to be involved in protein dephosphorylation and signal transduction. Located in plasma membrane. [provided by Alliance of Genome Resources, Feb 2025]

Synonyms

BAM32;

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Detailed Information

Dual Adaptor of Phosphotyrosine and 3-Phosphoinositides, commonly known as DAPP1, is a crucial signaling protein that plays a significant role in various cellular processes. Its unique name reflects its ability to simultaneously interact with phosphotyrosine residues on proteins and with 3-phosphoinositides in cell membranes, highlighting its versatile nature in cellular signaling. DAPP1 is a member of the Grb2-associated binder (GAB) family of adaptor proteins and is involved in the transduction of signals from activated receptors to downstream effectors. By bridging the gap between receptor tyrosine kinases and intracellular signaling pathways, DAPP1 serves as a pivotal regulator of cell proliferation, differentiation, and survival. Its ability to integrate signals from both tyrosine kinase receptors and phosphoinositide signaling pathways positions DAPP1 at a critical juncture in cellular communication.

Structure and Domain Organization of DAPP1

DAPP1 exhibits a complex and specialized structure tailored for its unique role in cellular signaling. At its core, DAPP1 features an N-terminal pleckstrin homology (PH) domain, responsible for its interaction with 3-phosphoinositides in the cell membrane.

Adjacent to the PH domain, DAPP1 contains a central Src homology 2 (SH2) domain, which enables its binding to phosphotyrosine residues on activated receptor tyrosine kinases and other signaling proteins.

Furthermore, DAPP1 possesses a proline-rich region at its C-terminus, facilitating interactions with proteins containing SH3 domains.

The intricate domain organization of DAPP1, comprising the PH, SH2, and proline-rich domains, underscores its versatility in integrating signals from both tyrosine kinase receptors and phosphoinositide signaling pathways.

Function of DAPP1

DAPP1 plays a pivotal role in cellular signaling cascades, acting as a central mediator in the integration of multiple signaling pathways. One of its primary functions is its involvement in receptor tyrosine kinase signaling, where it serves as a bridge between activated receptors and downstream effectors. DAPP1's ability to bind both phosphotyrosine residues on proteins and 3-phosphoinositides in the cell membrane enables it to coordinate intricate cellular responses.

DAPP1's role in signal transduction is particularly significant in immune cells, where it modulates processes such as B-cell receptor signaling. By linking B-cell receptors to phosphoinositide signaling, DAPP1 contributes to B-cell activation, differentiation, and antibody production. Additionally, DAPP1 is involved in chemokine receptor signaling, affecting immune cell migration and homing.

Furthermore, DAPP1 has been implicated in regulating cellular proliferation and survival pathways. Its interactions with key signaling molecules influence cell growth and differentiation, making it essential for normal cellular development and tissue homeostasis. DAPP1's involvement in both tyrosine kinase and phosphoinositide signaling pathways positions it at a critical juncture, allowing it to modulate various cellular processes, including cell adhesion, cytoskeletal rearrangement, and vesicular trafficking.

DAPP1 and Cancer

DAPP1 gene has been increasingly implicated in the occurrence and progression of various cancers. This gene plays a crucial role in cellular signaling pathways, specifically in the regulation of cell growth, differentiation, and migration. Abnormal expression or mutation of DAPP1 has been observed in various cancer types, including breast, colon, lung, and pancreatic cancer.

DAPP1 acts as an oncogene, promoting cancer development and progression. In normal cells, DAPP1 helps regulate cell growth and differentiation by modulating signaling pathways such as the MAPK and PI3K/Akt pathways. However, in cancer cells, dysregulated DAPP1 expression leads to uncontrolled cell proliferation and inhibits cell death, contributing to the formation of tumors.

Moreover, DAPP1 has been found to be involved in cancer metastasis. It interacts with integrins, a class of cell adhesion molecules that play a pivotal role in cell migration and invasion. Increased expression of DAPP1 leads to enhanced integrin function, thereby promoting metastasis to distant organs.

References:

Chen, Shilei et al. "Melatonin enhances thrombopoiesis through ERK1/2 and Akt activation orchestrated by dual adaptor for phosphotyrosine and 3-phosphoinositides." Journal of pineal research vol. 68,3 (2020): e12637. doi:10.1111/jpi.12637
Dowler, S et al. "DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides." The Biochemical journal vol. 342 (Pt 1),Pt 1 (1999): 7-12.

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