DAPL1

Official Full Name

death associated protein like 1

Organism

Homo sapiens

GeneID

92196

Background

Predicted to enable ribosome binding activity; translation initiation factor binding activity; and translation repressor activity. Predicted to be involved in several processes, including cellular response to amino acid starvation; negative regulation of CD8-positive, alpha-beta T cell activation; and negative regulation of metabolic process. Predicted to act upstream of or within cell population proliferation and gene expression. Predicted to be located in membrane. Predicted to be active in nucleus. [provided by Alliance of Genome Resources, Feb 2025]

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Detailed Information

Death Associated Protein-Like 1 (DAPL1) is a protein that has garnered significant attention in the field of cell biology and cancer research due to its potential implications in cell survival, apoptosis, and tumorigenesis.

Structure And Domain Organization of DAPL1

DAPL1 exhibits a distinct structural architecture that provides valuable insights into its potential functions and cellular roles. At the core of its structure lies a conserved Death Domain (DD), a characteristic feature of the Death Associated Protein (DAP) family, which suggests its involvement in apoptotic and cell death pathways. Adjacent to the DD, DAPL1 contains a coiled-coil domain, known for mediating protein-protein interactions. This domain likely enables DAPL1 to interact with various cellular partners, modulating its function in diverse signaling pathways.

Furthermore, DAPL1 possesses multiple ankyrin repeat domains, which are frequently involved in protein-protein interactions and are crucial for mediating specific protein associations. These ankyrin repeat domains potentially allow DAPL1 to interact with target proteins, participating in intricate cellular processes.

Additionally, DAPL1 contains a sterile alpha motif (SAM) domain, a protein interaction module often involved in homo- and hetero-oligomerization. The presence of the SAM domain in DAPL1 suggests its involvement in the formation of protein complexes, possibly regulating its function and localization within the cell.

Function of DAPL1

DAPL1 is a protein with diverse functions in cellular processes. Although its exact role is still under intensive research, emerging studies suggest its involvement in critical biological functions. DAPL1 is presumed to be associated with apoptotic pathways, implying a potential role in programmed cell death. Additionally, its interactions with other proteins in cellular signaling pathways indicate participation in intricate cellular processes, such as cell proliferation, differentiation, and survival.

Moreover, DAPL1 has been implicated in cytoskeletal dynamics, suggesting its involvement in regulating cell shape, adhesion, and motility. Its interactions with cytoskeletal components indicate a potential role in modulating cellular architecture and movement. Furthermore, recent research has indicated a possible association of DAPL1 with cancer. Altered expression levels of DAPL1 have been observed in various cancer types, suggesting its involvement in tumorigenesis and cancer progression.

Furthermore, DAPL1 has been proposed to have a role in neuronal development and functioning. Its expression patterns and interactions within neuronal cells imply a potential role in neuronal migration, differentiation, and synaptic plasticity.

In summary, DAPL1 appears to have multifaceted functions in different cellular contexts, including apoptosis, cytoskeletal regulation, cancer biology, and neurodevelopment. Further investigations are essential to unravel the precise mechanisms and signaling pathways through which DAPL1 operates, shedding light on its significance in normal physiology and disease states, potentially paving the way for targeted therapeutic interventions.

References:

Ma, Xiaoyin et al. "Regulation of cell proliferation in the retinal pigment epithelium: Differential regulation of the death-associated protein like-1 DAPL1 by alternative MITF splice forms." Pigment cell & melanoma research vol. 31,3 (2018): 411-422. doi:10.1111/pcmr.12676
Ma, Xiaoyin et al. "DAPL1 prevents epithelial-mesenchymal transition in the retinal pigment epithelium and experimental proliferative vitreoretinopathy." Cell death & disease vol. 14,2 158. 25 Feb. 2023, doi:10.1038/s41419-023-05693-4

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