NA14 Is a Novel Nuclear Autoantigen with a Coiled-coil Domain

Ramos‐Morales, Francisco; Infante, Carlos; Fedriani, Concepción; Bornens, Michel; Rı́os, Rosa M.

doi:10.1074/jbc.273.3.1634

Cited by 27 publications

(28 citation statements)

References 33 publications

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“…However, expression was not observed with the exception of DIP13-GFP (deflagellation induced protein of 13 kD), the Chlamydomonas homologue of human NA14 [Pfannenschmid et al, 2003]. This small coiled-coil protein was identified as an autoantigen in patients suffering from Sjogren's syndrome [Ramos-Morales et al, 1998] and is a component of the human centrosome [Andersen et al, 2003]. In moderately expressing strains, the fusion was targeted to the basal apparatus of C. reinhardtii whereas over-expression caused the formation of ectopic aggregates of DIP13-GFP and strongly reduced the amount of wild-type DIP13.…”

Section: Introductionmentioning

confidence: 91%

GFP as a tool for the analysis of proteins in the flagellar basal apparatus of Chlamydomonas

Schoppmeier

Mages

Lechtreck

2005

Cell Motil. Cytoskeleton

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Green fluorescent protein (GFP) was used to analyse three proteins in the flagellar basal apparatus of C. reinhardtii: (1) Striated fiber assemblin (SFA), the major component of the striated microtubule-associated fibers; (2) Centrin, present in the nucleus basal body connectors (NBBCs) and the distal connecting fiber (dCF) between the two basal bodies; and (3) DIP13, the Chlamydomonas homologue of human autoantigen NA14. The fusions co-localized with the wild-type proteins when expressed moderately. Overexpression of centrin-GFP and DIP13-GFP resulted in the formation of large aggregates and disturbed the distribution of the respective wild-type proteins. The amount of wild-type DIP13 was significantly reduced in cells overexpressing DIP13-GFP. Moreover, the cells frequently failed to assemble full-length flagella and flagellar regeneration was delayed, indicating a role of DIP13 during flagellar assembly. In contrast, overexpression of GFP-SFA, which retained more wild-type properties than SFA-GFP, increased the size of the striated fibers without altering the cross-shaped pattern. Abnormal patterns were observed in centrin-deficient cells, suggesting that centrin is required for proper localization of SFA. Photobleaching of GFP-SFA fibers indicated that GFP-SFA in the fibers is turned over slowly. Conditionally expressed centrin-GFP was incorporated into NBBCs in regions close to the basal bodies, but underrepresented in the dCF, indicative of a different dynamic of these two centrin fibers. Bending of the NBBCs was observed in vivo during flagellar motion, indicating that the filaments are flexible. In conclusion, in Chlamydomonas GFP-tagging is a useful tool for yielding new insights into the function and properties of the analyzed proteins.

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Section: Introductionmentioning

confidence: 91%

GFP as a tool for the analysis of proteins in the flagellar basal apparatus of Chlamydomonas

Schoppmeier

Mages

Lechtreck

2005

Cell Motil. Cytoskeleton

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“…In this report we describe a new component of the MT cytoskeleton that we call deflagellation-inducible protein of 13 kDa (DIP13). We have found DIP13 and its human counterpart NA14 (Ramos-Morales et al, 1998) associated with MTs both in flagellar axonemes and -obviously more concentrated -in basal bodies/centrioles in both organisms. Reducing the intracellular amount of DIP13 protein in Chlamydomonas by RNAi interfered with cell division, resulting in multinucleate, multiflagellate cells.…”

mentioning

confidence: 88%

“…Anti-NA14 polyclonal antibody has been described previously (Ramos-Morales et al, 1998). The antibody against C. reinhardtii α-tubulin used for indirect immunofluorescence has been described (Silflow and Rosenbaum, 1981) and mouse monoclonal antibody B- Fig.…”

Section: Antibodiesmentioning

confidence: 99%

ChlamydomonasDIP13 and human NA14: a new class of proteins associated with microtubule structures is involved in cell division

Pfannenschmid

Wimmer

Rios

et al. 2003

Journal of Cell Science

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We have cloned and characterized a single copy C. reinhardtii gene containing an open reading frame of 333 nucleotides encoding a 12.7 kDa protein. The novel protein, DIP13, exhibits 60% identity with two mammalian proteins, human NA14 and an unnamed mouse protein. Homologous sequences are also present in several protozoan, trematode and fish genomes, but no homologs have been found in the completed genomes of yeast, Drosophila, C. elegans and A. thaliana. By using a specific antibody we have localized DIP13 to microtubule structures, namely basal bodies, flagellar axonemes and cytoplasmic microtubules. Anti-DIP13 antibody also specifically recognized human NA14 by immunofluorescence and stained basal bodies and flagella of human sperm cells as well as the centrosome of HeLa cells. Expression of the DIP13 open reading frame in antisense orientation in Chlamydomonas resulted in multinucleate, multiflagellate cells,which suggests a role for this protein in ensuring proper cell division. Thus,DIP13/NA14 could represent the founding members of a new class of highly conserved proteins that are associated with microtubule structures.

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“…Transfected NA-14 localized to the nucleus; thus, NA-14 was reported as a nuclear autoantigen [19]. The physiological role of NA-14 remains unknown.…”

Section: Introductionmentioning

confidence: 98%

“…Nuclear autoantigen 14 kDa (NA-14)/Sjögren's syndrome nuclear antigen-1 (SSNA-1) was originally identified as a novel autoantigen recognized by autoimmune serum from a patient with SS [19]. Transfected NA-14 localized to the nucleus; thus, NA-14 was reported as a nuclear autoantigen [19].…”

Section: Introductionmentioning

confidence: 98%

A re-evaluation of anti-NA-14 antibodies in patients with primary Sjögren’s syndrome: Significant role of interferon-γ in the production of autoantibodies against NA-14

et al. 2016

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Novel autoantibodies against nuclear antigen of 14 kDa (NA-14)/Sjögren's syndrome nuclear antigen-1 (SSNA-1) are predominantly recognized in sera of patients with primary Sjögren's syndrome (pSS). However, the detailed characteristics of the anti-NA-14 antibody remain unknown. Here, we sought to clarify the characteristics of anti-SSNA-1/NA-14 antibodies and the mechanisms of autoantibody production using sera from patients with connective tissue diseases (including pSS), autoimmune sera reacting with standard autoantigens (SS-A/Ro and/or SS-B/La, ds DNA, Scl-70 and Jo-1), and normal healthy controls (NHCs). Anti-NA-14 antibodies were predominantly recognized in sera from patients with pSS and in autoimmune sera reacting with thSS-A/Ro and/or -SS-B/Lo. Indirect immunofluorescence analysis showed that NA-14 was strongly expressed in mitotic-phase cells. Patients with pSS having anti-NA-14 antibodies exhibited significant elevation of serum IP-10 and BAFF compared to that in patients with pSS without anti-NA-14 antibodies and NHCs. Thus, our data demonstrated that anti-NA-14 antibodies could be classified as novel autoantibodies reacting with mitosis-related autoantigens predominantly recognized in pSS. Moreover, interferon-γ played an important role in the production of anti-NA-14 autoantibodies as patients with pSS having anti-NA-14 antibodies exhibited increased serum levels of IP-10 and BAFF.

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NA14 Is a Novel Nuclear Autoantigen with a Coiled-coil Domain

Cited by 27 publications

References 33 publications

GFP as a tool for the analysis of proteins in the flagellar basal apparatus of Chlamydomonas

GFP as a tool for the analysis of proteins in the flagellar basal apparatus of Chlamydomonas

ChlamydomonasDIP13 and human NA14: a new class of proteins associated with microtubule structures is involved in cell division

A re-evaluation of anti-NA-14 antibodies in patients with primary Sjögren’s syndrome: Significant role of interferon-γ in the production of autoantibodies against NA-14

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