DAAM1

Official Full Name

dishevelled associated activator of morphogenesis 1

Organism

Homo sapiens

GeneID

23002

Background

Cell motility, adhesion, cytokinesis, and other functions of the cell cortex are mediated by reorganization of the actin cytoskeleton and several formin homology (FH) proteins have been associated with these processes. The protein encoded by this gene contains two FH domains and belongs to a novel FH protein subfamily implicated in cell polarity. A key regulator of cytoskeletal architecture, the small GTPase Rho, is activated during development by Wnt/Fz signaling to control cell polarity and movement. The protein encoded by this gene is thought to function as a scaffolding protein for the Wnt-induced assembly of a disheveled (Dvl)-Rho complex. This protein also promotes the nucleation and elongation of new actin filaments and regulates cell growth through the stabilization of microtubules. Alternative splicing results in multiple transcript variants encoding distinct proteins. [provided by RefSeq, Jul 2012]

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Detailed Information

Dishevelled Associated Activator of Morphogenesis 1 (DAAM1) is a pivotal adapter protein, belonging to the Dishevelled-associated activator of morphogenesis (DAAM) family. Much like its counterparts in the Grb7/Gr10/Grb14 protein family, DAAM1 interacts with various receptor tyrosine kinases, exerting profound influence over diverse signaling pathways within the cell.

Expression of DAAM1

Initially identified in multiple tissues, DAAM1 mRNA expression was found to be abundant in skeletal muscle, brain, heart, cartilage, and adipose tissue in mice. Similarly, in humans, DAAM1 exhibited higher expression in the pancreas and skeletal muscle, intermediate levels in the brain and cardiac muscle, and lower expression in tissues such as the liver, kidney, lung, placenta, spleen, prostate, ovary, colon, testis, and small intestine.

Structure of DAAM1

The protein structure of DAAM1 includes various domains such as the pleckstrin homology domain (PH), the N-terminal proline-rich region (PR), a Ras-associating domain (RA), a C-terminal Src homology 2 domain (SH2), and the family-specific BPS domain. These domains are pivotal in defining DAAM1's functions. For example, the SH2 domain allows DAAM1 to interact with phosphorylated tyrosine residues of other proteins, facilitating its role in various signaling pathways. Additionally, the BPS domain has been implicated in DAAM1's involvement in insulin signaling, where it interacts with insulin receptor (IR) and insulin-like growth factor 1 receptor (IGF1R), modulating essential cellular responses. DAAM1, like other methylated proteins, directs the nucleation and elongation of new actin filaments using its conserved methylated homology-2 (FH2) structural domain. It is a Rho-regulated protein that has been linked to the regulation of neuronal development and formation of the stomach. It has been identified as a binding protein for the Wnt receptor-associated protein Disheveled.

Function and Specificities of DAAM1

The multifaceted role of DAAM1 in cellular processes, encompasses cell proliferation, metabolism, and apoptosis. Notably, dysregulation of DAAM1 expression has been linked to specific disease contexts, including certain types of cancers. For instance, upregulation of DAAM1 mRNA has been detected in primary cervical squamous cell cancers. Experimental depletion of DAAM1 mRNA through siRNA techniques resulted in marked inhibition of cell growth in cervical squamous cell carcinoma, underscoring DAAM1's significance as a survival factor in this disease.

Figure 1. DAAM1 participates in the Wnt/PCR Pathway.

DAAM1 is a versatile adapter protein crucial in regulating diverse cellular processes and exhibits significant relevance in the context of cancer, specifically cervical squamous cell carcinoma. Its intricate regulatory mechanisms, coupled with its interactions in critical signaling pathways, highlight its importance in both normal cellular functions and disease contexts.

References:

Shi D .Planar cell polarity regulators in asymmetric organogenesis during development and disease[J].Journal of Genetics and Genomics,2023,50(02):63-76.
Ajima, R., Bisson, J.A., Helt, J.C., Nakaya, M.A., Habas, R., Tessarollo, L., He, X., Morrisey, E.E., Yamaguchi, T.P., Cohen, E.D., 2015. DAAM1 and DAAM2 are co-required for myocardial maturation and sarcomere assembly. Dev. Biol. 408, 126-139.

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