Novel Golgi Protein, GoPro49, Is a Specific Dental Follicle Marker

Takatalo, Maarit; Tümmers, Mark; Rönnholm, Ragna

doi:10.1177/0022034509338452

Cited by 14 publications

(14 citation statements)

References 18 publications

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“…A lack of a DIA1 homologue in nematodes may be related to some of the differences in neurobiology found in nematodes compared to other metazoans [70]–[74]. Our overall model is that DIA1 evolved in an ancestor of the cnidarians and, despite being ubiquitously expressed in mammalian tissues [39], [41], [75], gene loss has a marked impact on neurological function in humans, thereby probably causing the symptoms of ASD. Whatever the secretory-pathway role of DIA1 is, it is now defunct or significantly different, in nematodes.…”

Section: Discussionmentioning

confidence: 94%

Characterization of the Deleted in Autism 1 Protein Family: Implications for Studying Cognitive Disorders

2011

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Autism spectrum disorders (ASDs) are a group of commonly occurring, highly-heritable developmental disabilities. Human genes c3orf58 or Deleted In Autism-1 (DIA1) and cXorf36 or Deleted in Autism-1 Related (DIA1R) are implicated in ASD and mental retardation. Both gene products encode signal peptides for targeting to the secretory pathway. As evolutionary medicine has emerged as a key tool for understanding increasing numbers of human diseases, we have used an evolutionary approach to study DIA1 and DIA1R. We found DIA1 conserved from cnidarians to humans, indicating DIA1 evolution coincided with the development of the first primitive synapses. Nematodes lack a DIA1 homologue, indicating Caenorhabditis elegans is not suitable for studying all aspects of ASD etiology, while zebrafish encode two DIA1 paralogues. By contrast to DIA1, DIA1R was found exclusively in vertebrates, with an origin coinciding with the whole-genome duplication events occurring early in the vertebrate lineage, and the evolution of the more complex vertebrate nervous system. Strikingly, DIA1R was present in schooling fish but absent in fish that have adopted a more solitary lifestyle. An additional DIA1-related gene we named DIA1-Like (DIA1L), lacks a signal peptide and is restricted to the genomes of the echinoderm Strongylocentrotus purpuratus and cephalochordate Branchiostoma floridae. Evidence for remarkable DIA1L gene expansion was found in B. floridae. Amino acid alignments of DIA1 family gene products revealed a potential Golgi-retention motif and a number of conserved motifs with unknown function. Furthermore, a glycine and three cysteine residues were absolutely conserved in all DIA1-family proteins, indicating a critical role in protein structure and/or function. We have therefore identified a new metazoan protein family, the DIA1-family, and understanding the biological roles of DIA1-family members will have implications for our understanding of autism and mental retardation.

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Section: Discussionmentioning

confidence: 94%

Characterization of the Deleted in Autism 1 Protein Family: Implications for Studying Cognitive Disorders

2011

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“…In the pre-eruptive phase, the tooth remains cradled intra-osseously within a mesenchymal tissue, the dental follicle, which gives rise to the PDL tissue. F-spondin and Golgi protein 49kDa are expressed specifically in the dental follicle and in early PDL tissue in vivo (13, 59). The eruptive pre-functional phase starts when teeth begin to move toward the surface of the jaws.…”

Section: Factors Influencing Pdl Behavior In Vitromentioning

confidence: 99%

Implications of cultured periodontal ligament cells for the clinical and experimental setting: A review

Marchesan

Scanlon

Soehren

et al. 2011

Archives of Oral Biology

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The periodontal ligament (PDL) is a key contributor to the process of regeneration of the periodontium. The heterogeneous nature of the PDL tissue, its development during early adulthood, and the different conditions to which the PDL tissue is exposed to in vivo impart on the PDL unique characteristics that may be of consequence during its cultivation in vitro. Several factors affecting the in vivo setting influence the behavior of PDL fibroblasts in culture. The purpose of this review is to address distinct factors that influence the behavior of PDL fibroblasts in culture — in vivo-in vitro transitions, cell identification/isolation markers, primary PDL cultures and cell lines, tooth-specific factors, and donor-specific factors. Based on the reviewed studies, the authors recommendations include the use of several identification markers to confirm cell identity, use of primary cultures at early passage to maintain unique PDL heterogeneic characteristics, and noting donor conditions such as age, systemic health status, and tooth health status. Continued efforts will expand our understanding of the in vitro and in vivo behavior of cells, with the goal of orchestrating optimal periodontal regeneration. This understanding will lead to improved evidence-based rationales for more individualized and predictable periodontal regenerative therapies.

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“…DIA1 expression has been observed in cartilaginous mesenchymal tissues, regulated developmentally, with the highest expression seen in proliferating chondrocytes ( Takatalo et al, 2008 ). Further, colocalisation with beta-coatomer protein has been observed, and is suggestive of a function in secretory processes ( Takatalo et al, 2009 ). Then, characteristic expression of DIA1 has been observed in dental follicles, which may also suggest a role in secretion and trafficking ( Takatalo et al, 2009 ).…”

Section: Introductionmentioning

confidence: 99%

Phosphoproteomic insights into processes influenced by the kinase-like protein DIA1/C3orf58

Hareza

Bakun

Świderska

et al. 2018

PeerJ

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Many kinases are still ‘orphans,’ which means knowledge about their substrates, and often also about the processes they regulate, is lacking. Here, DIA1/C3orf58, a member of a novel predicted kinase-like family, is shown to be present in the endoplasmic reticulum and to influence trafficking via the secretory pathway. Subsequently, DIA1 is subjected to phosphoproteomics analysis to cast light on its signalling pathways. A liquid chromatography–tandem mass spectrometry proteomic approach with phosphopeptide enrichment is applied to membrane fractions of DIA1-overexpressing and control HEK293T cells, and phosphosites dependent on the presence of DIA1 are elucidated. Most of these phosphosites belonged to CK2- and proline-directed kinase types. In parallel, the proteomics of proteins immunoprecipitated with DIA1 reported its probable interactors. This pilot study provides the basis for deeper studies of DIA1 signalling.

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Novel Golgi Protein, GoPro49, Is a Specific Dental Follicle Marker

Abstract: Bsp1, bone sialoprotein 1; GoPro49, Golgi protein 49 kDa; E16, embryonic day 16; HERS, Hertwig's epithelial root sheath; PDL, periodontal ligament; dpn, day post-natal.

Cited by 14 publications

References 18 publications

Characterization of the Deleted in Autism 1 Protein Family: Implications for Studying Cognitive Disorders

Characterization of the Deleted in Autism 1 Protein Family: Implications for Studying Cognitive Disorders

Implications of cultured periodontal ligament cells for the clinical and experimental setting: A review

Phosphoproteomic insights into processes influenced by the kinase-like protein DIA1/C3orf58

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