|Written||2011-10||June L Traicoff, Stephen M Hewitt, Joon-Yong Chung|
|Center for Peer Review, Science Management, SRA International, Inc Maryland, USA (JLT); Applied Molecular Pathology Laboratory & Tissue Array Research Program, Laboratory of Pathology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA (SMH); Applied Molecular Pathology Laboratory, Laboratory of Pathology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA (JYC)|
(Note : for Links provided by Atlas : click)
|DnaJ (Hsp40) homolog|
|Location||16p13.3 [Link to chromosome band 16p13]|
|Location_base_pair||Starts at 4425805 and ends at 4456774 bp from pter ( according to hg19-Feb_2009) [Mapping DNAJA3.png]|
|Local_order||According to NCBI Map Viewer, genes flanking DNAJA3 are COR07-PAM16, NMRAL1, and HMOX2.|
|Chromosome 16 - NC_000016.9. Modified from NCBI Map Viewer.|
|Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)|
|CREBBP (16p13.3) / DNAJA3 (16p13.3)||DNAJA3 (16p13.3) / CREBBP (16p13.3)||DNAJA3 (16p13.3) / DNAJA3 (16p13.3)|
|DNAJA3 (16p13.3) / RAB5C (17q21.2)|
|Note||DNAJA3 was first identified by its ability to form complexes with the human papillomavirus E7 oncoprotein (Schilling et al., 1998) in a yeast-two hybrid screen. Sequence analysis revealed that DNAJA3 was the human homolog of the Drosophila tumor suppressor protein Tid56. Furthermore, DNAJA3 contained a J-domain which is characteristic of the family of DnaJ proteins which interact with and stimulate the ATPase activity of heat shock cognate 70 (hsc70) family members (Schilling et al., 1998).|
|Note|| DNAJA3 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins. There are 41 known DnaJ/Hsp40 proteins in the human genome (Qiu et al., 2006).
According to NCBI Gene, the DNAJA3 gene is conserved in human chimpanzee, cow, mouse, rat, chicken, zebrafish, fruit fly, mosquito, C. elegans, S. pombe, S. cerevisiae, K. lactis, E. gossypii, M. grisea, N. crassa, and rice.
|Description|| The DNAJA3 gene is located on chromosome 16p13.3 between markers D16S521 and D16S418. This chromosomal region carries several loci implicated in human proliferation disorders, including the tuberous sclerosis 2 gene (TSC2), polycystic kidney disease 1 gene (PKD1), and the CREB binding protein (CBP) locus (Yin and Rozakis-Adcock, 2001).|
DNAJA3 is approximately 34 kb and is composed of 12 exons separated by 11 introns. Exon sizes vary from 64 to 232 nucleotides, with the exception of exon 12 corresponding to the 3' untranslated region of DNAJA3, which extends over 1.1 kb. Intron sizes vary from 618 to 8291 nucleotides (Yin and Rozakis-Adcock, 2001).
Sequence encoding the DNAJ domain is present in exons 2, 3 and 4, sequence encoding the Cys-rich domain is found in exons 5 an 6, and the COOH-terminal region is found in exons 7 through 11 (Yin and Rozakis-Adcock, 2001).
|Transcription|| Promoter elements. DNAJA3 contains a putative transcriptional start site 21 nucleotides upstream of the initiating methionine. The presumptive promoter is characterized by the lack of TATA and CAAT motifs, and a high G+C content. The 5' flanking region contains several consensus binding sites for transcription factors that regulate gene expression during tissue and organ development, such as myeloid zinc finger (MZF1), Ikaros 2 and homeodomain proteins, as well as factors implicated in cell growth and survival responses, including AP-1, PEA3, E2F and NF-kB.|
Splice variants. Alternative splicing of a single heteronuclear RNA (hnRNA) species generates the three DNAJA3 isoforms. The long form DNAJA3L (hTID1L) fully incorporates all exons. The intermediate form DNAJA3I (hTID1I) is generated by splicing of exon 10 to exon 12. This results in the loss of the 34 C-terminal-most amino acids as well as the stop codon; these are replaced with six amino acids KRSTGN from exon 12. The short form DNAJA3S (hTID1S) results from an in-frame deletion of 50 amino acids that correspond precisely to exon 5 (Yin and Rozakis-Adcock, 2001).
RNA expression. DNAJA3 mRNA was detected in 50 different human fetal and adult tissues. However the relative abundance correlated with metabolic activity of the tissues, with the highest levels observed in liver and skeletal muscle (Kurzik-Dumke and Czaja, 2007). BR> Human tissues and cell lines showed differential expression of the three DNAJA3 splice variant mRNAs. Fetal brain tissue predominantly expressed DNAJA3I, while breast tissues and T-cells predominantly expressed DNAJA3L. Cell lines derived from prostate epithelia, skin and lung fibroblasts, normal astrocytes, and an osteosarcoma predominantly expressed DNAJA3I with low levels of DNAJA3L also present. DNAJA3S transcript was undetectable in all samples (Yin and Rozakis-Adcock, 2001).
DNAJA3 transcripts showed differential expression during development. Expression of DNAJA3 transcripts in mouse neonatal cardiomyocytes increased as development of the heart proceeded and reached a maximal level at 4 weeks of age, when cardiac myocytes have matured (Hayashi et al., 2006). DNAJA3 expression also increased in pathological cardiac hypertrophic states (Hayashi et al., 2006).
|Pseudogene||Paralogs. According to GeneCards, DNAJC16 is a paralog for DNAJA3. DNAJC16 is located on chromosome 1p36.1.|
|Note||The DNAJA3 gene encodes three cytosolic (Tid50, Tid48, Tid46) proteins and three mitochondrial (Tid43, Tid40, Tid38) proteins. Proteins encoded by the longer splice variant DNAJA3L have often been designated in the literature as Tid1L. Proteins encoded by the shorter splice variant DNAJA3S have often been named Tid1S. In this review, Tid1L will be designated DNAJA3L, and Tid1S will be designated DNAJA3S. Specific isoforms will be designated by size, e.g., Tid 50 will be designated as DNAJA3 (50 kD).|
|Description||DNAJA3 protein is present in two isoforms, corresponding to splice variants encoding them. The longer DNAJA3L isoform is a 480 amino acid protein with a predicted size of 52 kD. The shorter DNAJA3S isoform is a 453 amino acid protein with a predicted size of 49 kD (Lu et al., 2006; UniProt).|
|Expression||DNAJA3 protein has been detected in human breast, colon, ovarian, lung, and head and neck squamous cell carcinoma (HNSCC) tissues (Traicoff et al., 2007; Kurzik-Dumke et al., 2008; Chen et al., 2009).|
|Localisation||DNAJA3 localizes to human mitochondrial nucleoids, which are large protein complexes bound to mitochondrial DNA. Unlike other DnaJs, DNAJA3L and DNAJA3S form heterocomplexes; both unassembled and complexed DNAJA3 are observed in human cells. DNAJA3L showed a longer residency time in the cytosol prior to mitochondrial import as compared with DNAJA3S; DNAJA3L was also significantly more stable in the cytosol than DNAJA3S, which is rapidly degraded (Lu et al., 2006).|
|Function|| I. Binding partners|
Human DNAJA3 protein has been shown to interact with diverse partners, including viral proteins, heat shock proteins, and key regulators of cell signaling and growth.
Hepatitis B virus core protein: DNAJA3 associated with the hepatitis B virus core protein, specifically with the carboxyl-terminal region (amino acids 94-185). The N-terminal end of DNAJA3 (amino acids 1-447) was required for this interaction. Furthermore, the DNAJA3S precursor co-sedimented with viral capsid-like particles composed of the full-length core protein (Sohn et al., 2006). Interaction between DNAJA3 and the HBV core protein was confirmed in co-immunoprecipitation experiments using transfected hepatoma cells (Sohn et al., 2006).
Heat shock proteins
Hsp70 and Hsc70: endogenous DNAJA3 (specifically the cytosolic form) immunoprecipitated with the heat shock proteins Hsp70 and Hsc70 in normal colon epithelium and colon cancer cell lines (Kurzik-Dumke and Czaja, 2007). Endogenous DNAJA3 also interacted with Hsp70/Hsc70 in HEp2 cells, and this interaction was reduced in cells treated with interferon-gamma (Sarkar et al., 2001). The J domain of DNAJA3 was shown to be required for interaction with Hsp70 in HEK cells (Cheng et al., 2001).
Tumor suppressor proteins
Adenomatous polyposis coli (APC): endogenous cytosolic DNAJA3 proteins interacted with APC in normal colon epithelium and colorectal cancer cell lines (HT-29, Caco-2, and HRT-18). The N-terminal Armadillo domain of APC was sufficient for binding to DNAJA3. The DNAJA3 and APC interaction comprised part of a larger multi-component complex that also contained Hsp70, Hsc70, Actin, Dvl, and Axin. This complex functions independently of the known roles of APC in beta-catenin degradation and proliferation mediated by Wg/Wnt signaling (Kurzik-Dumke and Czaja, 2007).
Interferon-gamma receptor (IFN-gammaR) subunit IFN-gammaR2: DNAJA3 interacted with IFN-gamma R2 in transfected COS cells. Furthermore, DNAJA3 bound more efficiently to a IFN-gammaR2 chimera with an active kinase domain than to a similar construct with an inactive kinase domain (Sarkar et al., 2001).
NF-kappaB: DNAJA3 strongly associated with the cytoplasmic protein complex of NF-kappaB-IkappaB through direct interaction with IkappaBalpha/IkappaBbeta and the IKKalpha/beta subunits of the IkappaB kinase complex. The endogenous interaction was observed in Jurkat, SAOS-2, and HEK293 cells (Cheng et al., 2005).
DNA replication proteins
DNA polymerase gamma (Polga) alpha subunit: endogenous DNAJA3 interacted with the alpha subunit of Polga in HEK293 cells. Polga is the only mitochondrial DNA polymerase responsible for all mitochondrial DNA synthetic reactions (Hayashi et al., 2006).
II. Signaling pathways and cellular effects
DNAJA3 modulates diverse signaling pathways and cellular effects that are vital for cell growth and differentiation.
Neuromuscular synaptogenesis: DNAJA3 is an essential component of the agrin signaling pathway that is crucial for synaptic development. Motoneuron-derived agrin clusters nicotinic acetylcholine receptors (AChRs) in mammalian cells. DNAJA3 binds to the cytoplasmic domain of muscle-specific kinase (MuSK), a component of the agrin receptor and colocalizes with AchRs at developing, adult, and denvervated motor endplates. DNAJA3 transduces signals from MuSK activation to AchR clustering, culmintating in cross-linking to the subsynaptic cytoskeleton, as demonstrated by knockdown and overexpression experiments.
Hepatitis B virus replication: expression of DNAJA3 suppressed replication of HBV in human hepatoma cells, while knockdown of DNAJA3 led to increased HBV replication. The mechanism for inhibited replication was through accelerated degradation and destabilization of the viral core and HBx proteins (Sohn et al., 2006).
Motility and metastasis
DNAJA3 was shown to negatively regulate the motility and metastasis of breast cancer cells through attenuation of nuclear factor kappaB activity on the promoter of the IL8 gene (Kim et al., 2005). Reductions of DNAJA3 levels in MDA-MB231 breast cancer cells increased their migration as a result of increased interleukin-8 (IL-8) secretion without affecting survival or growth rate. Furthermore, DNAJA3 was shown to negatively modulate de novo synthesis of IL-8 through regulating NFkappaB activity. Additionally, DNAJA3 knockdown enhanced the metastasis of breast cancer cells in animals (Kim et al., 2005).
DNAJA3 encodes two mitochondrial matrix localized splice variants: DNAJA3 (43 kD) and DNAJA3 (40 kD). DNAJA3 (43 kD) and DNAJA3 (40 kD) do not themselves induce apoptosis; instead they have opposing effects on apoptosis induced by exogenous stimuli.
Although DNAJA3 has many cellular functions, DNAJA3 often localizes to the mitochondria and also has important functions in the mitochondria.
Tumor suppressor pathways
APC: DNAJA3 directly bound to the APC tumor suppressor protein and promoted a physiological function for APC that was independent of APC's involvement in beta-catenin degradation or regulation of the actin cytoskeleton (Kurzik-Dumke and Czaja, 2007).
Erb-B2/HER2: DNAJA3 physically interacted with the signaling domain of ErbB-2 and ErbB-2 were shown to colocalize in mammary carcinoma cells (SK-BR-3). Overexpression of DNAJA3 induced growth arrest and apoptosis in ErbB-2-overexpressing breast cancer cells; the DNAJ and C-terminal domains of DNAJA3 were critical for mediating apoptosis. Downregulation of ERK1/ERK2 and BMK1 MAPK pathways also contributed to apoptosis. DNAJA3S negatively regulated ErbB-2 signaling pathways by enhancing the degradation of ErbB-2. Finally, increased cellular DNAJA3 inhibited the growth of ErbB-2-dependent tumors in mice (Kim et al., 2004).
DNAJA3 was shown to be required for the T-cell transition from double-negative 3 to double-positive stages. Mice with dnaja3 specifically deleted in T cells developed thymic atrophy, with dramatic reduction of double-positive and single-positive thymocytes in the dnaja3(-/-) thymus. DNAJA3 deficiency inhibited cell proliferation and enhanced cell death of DN4 cells. The expression profile of genes involved in cytokine receptor signaling was altered in DN4 T-cells. Expression of human bcl-2 transgene restored T lymphocyte proliferation and differentiation in the dnaja3 knockout mice. These results suggest that dnaja3 is critical in early thymocyte development, especially during transition from the DN3 to double-positive stages, possibly through its regulation of bcl-2 expression, which provides survival signals.
|Homology|| Mouse (laboratory): Dnaja3 |
Dog (domestic): DNAJA3
|Note||The SF767 glioma cell line exhibits an aberrant 52 kD molecular weight protein. Sequence analysis of cDNA generated from this line showed two mutations: an additional thymine at nucleotide position 1438 and an additional cytosine at nucleotide position 1449. These mutations alter the reading frame of the DNAJA3 sequence, introducing an additional 71 amino acids following the penultimate threonine residue at position 479. The mutations appear to increase the steady-state abundance of the mutant protein, resulting in aberrantly high levels of the DNAJA3 mutant variant (Trentin et al., 2004).|
5. Implicated in
|Disease|| DNAJA3 and INT6 protein levels, as well as DNAJA3 and Patched protein levels, were positively correlated in human colon tumor tissues (Traicoff et al., 2007). However, there were no correlations between DNAJA3 and p53, c-Jun, or phospho-c-Jun protein levels (Traicoff et al., 2007). These results were demonstrated by multiplex tissue immunoblotting of tissue microarrays (Traicoff et al., 2007).|
Progression of colorectal cancers correlated with overexpression and loss of polarization of expression of DNAJA3. These changes were associated with upregulation of Hsp70 and loss of compartmentalization of APC (Kurzik-Dumke et al., 2008).
|Disease|| DNAJA3 protein expression showed a strong correlation with negative or weakly positive expression of ErbB2 in human breast cancer tissue samples. High DNAJA3 levels were strongly correlated with high levels of CHIP (carboxyl terminus of heat shock cognate 70 interacting protein). Lower expression of DNAJA3 had a higher risk of unfavorable tumor grade, later pathological stage, larger tumor size, and microscopic features of a more malignant histology (Jan et al., 2011). Higher expression of DNAJA3 correlated with increased 10-year overall and disease-free survival rate (Jan et al., 2011). |
The expression of the three DNAJA3 isoform transcripts was examined in human breast cancer carcinomas by RT-PCR. Aberrant expression of all three forms correlated with malignant transformation. Furthermore, elevated DNAJA3L expression was associated with less aggressive tumors (Kurzik-Dumke et al., 2010). Immunohistochemical analysis demonstrated high levels of DNAJA3 protein in tumors of the luminal A subtype, but significantly lower levels of DNAJA3 protein in the luminal B subtype, triple negative tumors, and the HER-2 subtype which overexpresses HER-2 (Kurzik-Dumke et al., 2010).
Multiplex tissue immunoblotting of human breast tumor tissue microarrays was used to test correlations between DNAJA3 protein levels and a set of tumor suppressor proteins. DNAJA3 protein levels showed strongly positive correlations with p53, Patched, and INT6 proteins (Traicoff et al., 2007). Additionally, DNAJA3 protein levels showed moderate positive correlations with c-Jun and phospho-c-Jun proteins (Traicoff et al., 2007).
|Entity||Head and neck squamous cell carcinoma (HNSCC)|
|Disease||The clinical association between DNAJA3 expression and progression of HNSCC was explored using immunohistochemical analysis of primary HNSCC patient tumor tissue. DNAJA3 expression was negatively associated with tumor T stage, overall stage, survival, and recurrence. Patients with higher expression of DNAJA3 were predicted to have better overall survival than those with low or undetectable expression of DNAJA3 protein (Chen et al., 2009). Highly malignant HNSCC cell lines also demonstrated low or undetectable levels of DNAJA3, in contrast to less aggressive lines where DNAJA3 protein was easily detected (Chen et al., 2009).|
|Disease||Multiplex tissue immunoblotting of ovarian tumor tissues demonstrated that DNAJA3 protein levels showed moderate positive correlations with INT6, c-Jun, phospho-c-Jun, and p53. No correlations were observed between DNAJA3 and Patched (Traicoff et al., 2007).|
|Disease||Multiplex tissue immunoblotting of lung tumor tissues demonstrated that DNAJA3 protein levels were strongly correlated with INT6. DNAJA3 protein levels were moderately correlated with Patched, c-Jun, and p53. However, DNAJA3 proteins showed negative correlation with phospho-c-Jun in these samples (Traicoff et al., 2007).|
|Note||Mice deficient in Dnaja3 developed dilated cardiomyopathy (DCM) and died before 10 weeks of age (Hayashi et al., 2006). Progressive respiratory chain deficiency and decreased copy number of mitochondrial DNA were observed in cardiomyocytes lacking Dnaja3 (Hayashi et al., 2006).|
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|This paper should be referenced as such :|
|Traicoff, JL ; Hewitt, SM ; Chung, JY|
|DNAJA3 (DnaJ (Hsp40) homolog, subfamily A, member 3)|
|Atlas Genet Cytogenet Oncol Haematol. 2012;16(3):196-204.|
|Free journal version : [ pdf ] [ DOI ]|
|On line version : http://atlasgeneticsoncology.usal.es/classic/Genes/DNAJA3ID40342ch16p13.html|
8. Other Leukemias implicated (Data extracted from papers in the Atlas) [ 2 ]
9. External links
|REVIEW articles||automatic search in PubMed|
|Last year publications||automatic search in PubMed|
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