DAPK3

Official Full Name

death associated protein kinase 3

Organism

Homo sapiens

GeneID

1613

Background

Death-associated protein kinase 3 (DAPK3) induces morphological changes in apoptosis when overexpressed in mammalian cells. These results suggest that DAPK3 may play a role in the induction of apoptosis. [provided by RefSeq, Jul 2008]

Synonyms

DLK; ZIP; ZIPK;

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Detailed Information

Death-Associated Protein Kinase 3 (DAPK3), also known as ZIP kinase (ZIPK), is a serine/threonine kinase that belongs to the Death-Associated Protein Kinase (DAPK) family. DAPK3 plays a significant role in diverse cellular processes, including apoptosis, autophagy, and cytoskeletal regulation. Unlike other members of the DAPK family, DAPK3 is primarily involved in non-apoptotic cell death pathways and is implicated in various physiological and pathological conditions. Its unique function in modulating cell death processes and its interactions with cytoskeletal components highlight its importance in maintaining cellular homeostasis. DAPK3 gene modulates various cellular processes, including apoptosis, autophagy, and inflammation. Alterations in DAPK3 expression or function can lead to imbalances in these processes, resulting in pathological conditions.

Structural of DAPK3

DAPK3 exhibits a well-defined structural organization, indicative of its diverse cellular functions. At the core of its structure allowing DAPK3 to phosphorylate specific substrates involved in various cellular processes. Adjacent to the catalytic domain, DAPK3 possesses a calmodulin-binding domain, enabling its regulation by calcium signaling. Calmodulin binding to this domain modulates DAPK3's activity, linking its function to intracellular calcium levels.

Additionally, DAPK3 contains a unique domain called the Death-Associated Protein Kinase-Related Autophagy Regulator (DRAAR) domain. This domain is specific to the DAPK family and plays a crucial role in autophagy induction. The DRAAR domain allows DAPK3 to interact with autophagic proteins, promoting the initiation of autophagy, a cellular process involved in degradation and recycling of cellular components.

Furthermore, DAPK3 features a coiled-coil region, which facilitates protein-protein interactions. This region is essential for mediating DAPK3's interactions with cytoskeletal proteins, such as myosin regulatory light chain (MRLC), leading to cytoskeletal rearrangements that influence cell shape and motility.

The intricate domain organization of DAPK3 highlights its versatility, allowing it to participate in diverse cellular pathways, including apoptosis, autophagy, and cytoskeletal regulation.

Function of DAPK3

Death-Associated Protein Kinase 3 (DAPK3), also known as ZIP kinase (ZIPK), serves as a multifaceted regulator in diverse cellular processes. One of its central functions is its involvement in the regulation of cell death and survival pathways. DAPK3 plays a pivotal role in non-apoptotic forms of cell death, such as autophagy and necrosis, by modulating the activity of key proteins involved in these processes. Moreover, DAPK3 has been identified as a crucial regulator of cytoskeletal dynamics. It phosphorylates various cytoskeletal proteins, including myosin regulatory light chain (MRLC) and vimentin, leading to changes in cell shape, motility, and adhesion. These cytoskeletal modifications are essential for processes like cell migration, invasion, and cytokinesis. Additionally, DAPK3 has been implicated in the regulation of inflammation, immune responses, and tissue remodeling, further underscoring its significance in maintaining cellular homeostasis. Dysregulation of DAPK3 has been linked to several diseases, including cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target for various pathological conditions.

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