Alternative titles; symbols
Other entities represented in this entry:
HGNC Approved Gene Symbol: TRIP11
SNOMEDCT: 42725006;
Cytogenetic location: 14q32.12 Genomic coordinates (GRCh38): 14:91,965,991-92,040,059 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 14q32.12 | Achondrogenesis, type IA | 200600 | Autosomal recessive | 3 |
| Odontochondrodysplasia 1 | 184260 | Autosomal recessive | 3 |
TRIP11 was first identified through its ability to interact functionally with thyroid hormone receptor-beta (THRB; 190160). It has also been found in association with the Golgi apparatus and microtubules.
Lee et al. (1995) used the yeast interaction trap, a version of the yeast 2-hybrid system, to identify proteins that specifically interact with the ligand-binding domain of rat thyroid hormone receptor-beta. They isolated HeLa cell cDNAs encoding several different thyroid receptor-interacting proteins (TRIPs), including TRIP11. TRIP11 interacted with rat Thrb only in the presence of thyroid hormone. It also showed a ligand-dependent interaction with RXR-alpha (RXRA; 180245), but did not interact with the glucocorticoid receptor (NR3C1; 138040) under any condition.
Using the yeast 2-hybrid system to identify proteins that bind specifically to an N-terminally truncated form of RB (RB1; 614041), p56(RB), Durfee et al. (1993) isolated several human cDNA clones encoding RB-interacting proteins, including the partial cDNA C5. By screening a human fibroblast cDNA library with the partial C5 cDNA, Chang et al. (1997) isolated a full-length coding sequence. The deduced 1,978-amino acid protein, which the authors called TRIP230, has a calculated molecular mass of approximately 230 kD. Northern blot analysis of 2 human cell lines detected 2 major TRIP230 transcripts of 6.3 kb and 4 kb.
Abe et al. (1997) stated that the 5-prime region of TRIP11, which they designated CEV14, encodes a predicted leucine zipper motif. Northern blot analysis detected CEV14 expression in all human tissues examined, with highest levels in heart, muscle, and pancreas, and lowest levels in lung and liver.
Ramos-Morales et al. (2001) cloned 2 splice variants of TRIP11, which they called GMAP210 and GMAP200, from a HeLa cell expression library screened with autoimmune serum from a patient with Sjogren syndrome (270150). The deduced 1,979-amino acid protein has an N-terminal domain containing 2 acidic nonhelical regions and a small coiled-coil domain followed by a long central coiled-coil region. The GMAP200 variant arises from alternative splicing of exon 4 and results in a protein that lacks amino acids 105-196. GMAP200 is predicted to contain a single acidic nonhelical region and a smaller coiled-coil domain in the N terminus. RT-PCR showed expression of both variants in HeLa cells.
Smits et al. (2010) noted that TRIP11 contains an N-terminal amphipathic lipid sensor (ALPS) domain, a long central coiled-coil domain, and a C-terminal GRIP-related Arf-binding (GRAB) domain.
Using exon-spanning RT-PCR to analyze TRIP11 in human chondrogenic cells derived from primary fibroblasts, Wehrle et al. (2019) detected abundant full-length mRNA as well as transcripts lacking exon 9 and carrying a shorter 5-prime end. The cDNA of the natural isoform predicts a 190-kD GMAP protein lacking the N terminus, which the authors designated GMAP190. The abundance of both isoforms increased continuously during chondrogenic differentiation and was highest when cells reached the hypertrophic stage. The same distribution of TRIP11 mRNA isoforms was found in primary human articular chondrocytes from healthy donors.
Ramos-Morales et al. (2001) determined that the TRIP11 gene consists of 21 exons and spans at least 70 kb. Analysis of the proximal promoter region identified a TATA box and putative binding sites for several regulatory elements.
By somatic cell hybrid analysis, Chang et al. (1997) mapped the TRIP11 gene to chromosome 14. They localized the TRIP11 gene to chromosome 14q31 using in situ hybridization. By FISH analysis, Abe et al. (1997) mapped the TRIP11 gene to chromosome 14q32.
Chang et al. (1997) noted that the very C-terminal region of TRIP230 is identical to the polypeptide fragment TRIP11 (Lee et al., 1995). Thus, they concluded that TRIP230 is able to interact with both RB and TR. TRIP230 uses 2 distinct regions to bind to RB and TR, respectively. TRIP230 binds to RB independently of thyroid hormone, whereas it forms a complex with TR in a thyroid hormone-dependent manner. Ectopic expression of the TRIP230 protein in cells, but not of a mutant form of TRIP230 that does not bind to TR, specifically enhanced TR-dependent transcriptional activity. Coexpression of wildtype RB, but not of mutant RB that fails to bind to TRIP230, inhibited such activity. Chang et al. (1997) stated that these results identify TRIP230 as a coactivator molecule that modulates TR activity, and uncover a role for RB in a pathway that responds to thyroid hormone.
Infante et al. (1999) found interaction between endogenous GMAP210 and microtubules in HeLa cells by cosedimentation, and confirmed interaction with use of microtubule polymerizing and disrupting agents. Using truncation mutants in microtubule binding assays, they mapped microtubule binding to the final 250 amino acids of the basic C-terminal domain. Likewise, the first 375 N-terminal amino acids were found to bind Golgi membranes. Immunolocalization of overexpressed GMAP210 perturbed the organization of the Golgi apparatus, causing dramatic enlargement, fragmentation, and distortion. Microtubules were also randomly distributed. Overexpression of the N terminus resulted in labeling of the Golgi apparatus, but had no effect on Golgi or microtubule structure. Overexpression of the C-terminal microtubule-binding domain led to centrosome labeling, suggesting specific binding to the minus ends of microtubules. Ramos-Morales et al. (2001) determined that overexpression of GMAP200 resulted in similar Golgi disruption, but weaker Golgi membrane binding, than that found by Infante et al. (1999) with GMAP210.
Rios et al. (2004) showed that GMAP210 recruited gamma-tubulin (see 191135)-containing complexes to Golgi membranes, even in conditions where microtubule polymerization was prevented and independently of Golgi apparatus localization within the cell. Under overexpression conditions, very short microtubules, or tubulin oligomers, were stabilized on Golgi membranes. GMAP210 depletion by RNA interference resulted in extensive fragmentation of the Golgi apparatus, supporting a role for GMAP210 in Golgi ribbon formation. Targeting of GMAP210 or its C terminus to mitochondria induced the recruitment of gamma-tubulin to the mitochondria surface and redistribution of mitochondria to a pericentrosomal location. The results suggested that GMAP210 displays microtubule anchoring and membrane fusion activities, thus contributing to the assembly and maintenance of the Golgi ribbon around the centrosome.
Drin et al. (2008) examined the attachment of golgin GMAP210 to lipid membranes. GMAP210 connected highly curved liposomes to flatter ones. This asymmetric tethering relied on motifs that sensed membrane curvature both in the N terminus of GMAP210 and in ARFGAP1 (608377), which controlled the interaction of the C terminus of GMAP210 with the small guanine nucleotide-binding protein ARF1 (103180). Drin et al. (2008) concluded that because membrane curvature constantly changes during vesicular trafficking, this mode of tethering suggests a way to maintain the Golgi architecture without compromising membrane flow.
Wong and Munro (2014) selected 10 mammalian golgins that are conserved outside of vertebrates and found on different regions of the Golgi and ectopically expressed them at the mitochondria through attachment to a mitochondrial transmembrane domain in place of their C-terminal Golgi targeting domain. The authors then used the distribution of cargo-laden vesicles originating from different locations as a readout for the golgins' tethering activity. Wong and Munro (2014) found that golgin-97 (GOLGA1; 602502), golgin-245 (GOLGA4; 602509), and GCC88 (607418) were able to capture endosome-to-Golgi cargoes; GM130 (GOLGA2; 602580) and GMAP210 (TRIP11) were able to capture endoplasmic reticulum (ER)-to-Golgi cargoes; and golgin-84 (GOLGA5; 606918), TMF1 (601126), and GMAP210 were able to capture Golgi resident proteins. Furthermore, electron microscopy yielded ultrastructural evidence for the accumulation of vesicular membranes around mitochondria decorated with specific golgins. Wong and Munro (2014) concluded that these data suggested that not only do the golgins capture vesicles, they also exhibit specificity toward vesicles of different origins: from the endosomes, from the ER, or from within the Golgi itself.
Abe et al. (1997) reported that in a patient with acute myelogenous leukemia (AML; 601626), the TRIP11 gene, which they called CEV14, was fused to the PDGFR-beta (PDGFRB; 173410) gene as a result of a t(5;14)(q33;q32) translocation. On initial diagnosis, this patient had exhibited a sole t(7;11) translocation, but the t(5;14)(q33;q32) translocation appeared during the relapse phase. The CEV14-PDGFRB chimeric gene consisted of the 5-prime region of CEV14 fused to the 3-prime region of PDGFRB.
Achondrogenesis, Type IA
Noting similarities between the skeletal and cellular phenotype of Trip11-null mice and patients with achondrogenesis type IA (ACG1A; 200600), Smits et al. (2010) sequenced the TRIP11 gene in 10 unrelated patients with ACG1A and identified homozygous or compound heterozygous loss-of-function mutations in all 10 patients, including 5 nonsense, 4 frameshift, and 2 splice site mutations (see, e.g., 604505.0001-604505.0004). The authors noted that some mutations were found in more than 1 family.
By whole-exome sequencing, Vanegas et al. (2018) identified compound heterozygous frameshift mutations (604505.0010 and 604505.0013) in the TRIP11 gene in a male infant, born of nonconsanguineous Colombian parents, with ACG1A. The mutations, which were confirmed by Sanger sequencing, segregated with the phenotype in the family.
Odontochondrodysplasia 1
Wehrle et al. (2019) analyzed the TRIP11 gene in 10 patients from 7 families with odontochondrodysplasia (ODCD1; 184260) and identified compound heterozygous mutations in all 10 (see, e.g., 604505.0001 and 604505.0005-604505.0012). The mutations segregated with disease in each family and were not found in public variant databases. Mutation analysis in patient fibroblasts demonstrated that all ODCD1 patients were compound heterozygous for a null mutation and a splice variant, with the latter being translated into low-abundance GMAP protein. Although all disease-associated TRIP11 mutations caused strong reduction of GMAP210, longer exposure revealed the presence of residual protein in cells from patients with ODCD1, whereas there was nearly complete loss of protein in cells from patients with ACG1A.
Wehrle et al. (2019) described a genotype/phenotype correlation associated with mutations in the TRIP11 gene, with ACG1A representing a null phenotype and ODCD being caused by hypomorphic TRIP11 mutations. Analysis of TRIP11-mutant primary cells revealed that Golgi organization, global secretory capacity, and IFT20 (614394) Golgi targeting are preserved in ODCD, but lost in ACG1A. However, in both mild and severe disease, mutations of TRIP11 impair Golgi glycan processing and synthesis of glycosylated cartilage matrix proteins, specifically disrupting hypertrophic chondrocyte differentiation in skeletal development.
By N-ethyl-N-nitrosourea (ENU) mutagenesis, Smits et al. (2010) identified mice with an autosomal recessive neonatal lethal phenotype involving short limbs, small thoracic cage, short snout, domed skull, and in some cases, omphalocele. Skeletal preparations revealed delayed mineralization of intramembranous and endochondral bone. Newborn mutant mice lacked vertebral-body ossification, and alveolar formation in the lungs was decreased compared to wildtype newborns. Whole genome SNP mapping identified a 3.7-Mb interval on mouse chromosome 12, and sequence analysis of candidate genes identified a leu1668-to-ter (L1668X) mutation in the Trip11 gene in mutant mice. Immunoblotting confirmed that GMAP210 was absent from mutant cells. Transmission electron microscopy revealed that Golgi architecture was disturbed in multiple tissues, including cartilage, and skeletal development was severely impaired, with chondrocytes showing swelling and stress in the endoplasmic reticulum, abnormal cellular differentiation, and increased cell death. Golgi-mediated glycosylation events were altered in fibroblasts and chondrocytes lacking GMAP210, and mutant chondrocytes had intracellular accumulation of the extracellular matrix protein perlecan (142461) but not of type II collagen or aggrecan. Smits et al. (2010) noted similarities between the features of Trip11-null mice and achondrogenesis type IA.
Achondrogenesis, Type IA
In 10 unrelated patients with type IA achondrogenesis (ACG1A; 200600), Smits et al. (2010) analyzed the TRIP11 gene and identified homozygosity or compound heterozygosity for various loss-of-function mutations, including an arg264-to-ter (R264X) substitution in exon 6. Zygosity for this mutation was not reported.
Odontochondrodysplasia 1
For discussion of the c.790C-T transition (c.790C-T, NM_004239.3) in exon 5 of the TRIP11 gene, resulting in an R264X substitution, that was found in compound heterozygosity in 3 Thai sibs (family 7, patients 8, 9 and 10) with odontochondrodysplasia (ODCD1; 184260) by Wehrle et al. (2019), see 604505.0005.
In 10 unrelated patients with type IA achondrogenesis (ACG1A; 200600), Smits et al. (2010) analyzed the TRIP11 gene and identified homozygosity or compound heterozygosity for various loss-of-function mutations, including a trp1224-to-ter (W1224X) substitution in exon 11. Zygosity for this mutation was not reported.
In 10 unrelated patients with type IA achondrogenesis (ACG1A; 200600), Smits et al. (2010) analyzed the TRIP11 gene and identified homozygosity or compound heterozygosity for various loss-of-function mutations, including a -2A-G transition (202-2A-G) in intron 2. Zygosity for this mutation was not reported.
In 10 unrelated patients with type IA achondrogenesis (ACG1A; 200600), Smits et al. (2010) analyzed the TRIP11 gene and identified homozygosity or compound heterozygosity for various loss-of-function mutations, including a change in exon 11 that resulted in a frameshift and premature termination: Asn701SerfsTer13. Zygosity for this mutation was not reported.
In 3 sibs from a Thai family (patients 8, 9, and 10) with odontochondrodysplasia (ODCD1; 184260), as well as an affected 3-year-old English boy (patient 4) and a 16-year-old Argentinian girl (patient 7), Wehrle et al. (2019) identified compound heterozygosity for a c.586C-T transition (c.586C-T, NM_004239.3) in exon 4 of the TRIP11 gene, resulting in a gln196-to-ter (Q196X) substitution, and another mutation in TRIP11. In the Thai sibs, the second mutation was another nonsense mutation (R264X; 604505.0001); in the Argentinian girl, it was a 2-bp deletion (c.2993_2994delAA; 604505.0006) in exon 11, predicted to result in a premature termination codon (Lys998SerfsTer5); and in the English boy, it was a c.4534C-T transition in exon 11, resulting in a gln1512-to-ter (Q1512X; 604505.0007) substitution. Analysis of fibroblasts from patient 10 revealed abrogation of a splice donor site by the Q196X mutation, causing complete in-frame skipping of exon 4; quantitative analysis showed that the amount of mutant protein (designated GMAP200) was approximately 30% of the amount of wildtype protein observed in controls. Immunofluorescence microscopy showed less intense GMAP staining in patients than in controls, but RGB profile plots demonstrated that the residual protein was still correctly targeted to the cis-Golgi, and a close-to-normal ribbon morphology was seen in patient 10 compared to patients with lower amounts of residual GMAP protein. Overexpression of the GMAP200 variant restored normal Golgi organization in GMAP210-deficient cells, consistent with some residual function. Mutant fibroblast-induced chondrocytes formed significantly fewer and smaller chondrogenic nodules, indicating that the production of bulk glycosylated proteoglycans was disrupted.
For discussion of the 2-bp deletion (c.2993_2994delAA, NM_004239.3) in exon 11 of the TRIP11 gene, causing a frameshift predicted to result in a premature termination codon (Lys998SerfsTer5), that was found in compound heterozygous state in a 16-year-old Argentinian girl (patient 7) with odontochondrodysplasia (ODCD1; 184260) by Wehrle et al. (2019), see 604505.0005.
For discussion of the c.4534C-T transition (c.4534C-T, NM_004239.3) in exon 11 of the TRIP11 gene, resulting in a gln1512-to-ter (Q1512X) substitution, that was found in compound heterozygous state in a 3-year-old English boy (patient 4) with odontochondrodysplasia (ODCD1; 184260) by Wehrle et al. (2019), see 604505.0005.
In 2 unrelated 17-year-old Turkish girls (patients 3 and 5) with odontochondrodysplasia (ODCD1; 184260), Wehrle et al. (2019) identified compound heterozygosity for a c.1228G-T transversion (c.1228G-T, NM_004239.3) in exon 9 of the TRIP11 gene, predicted to result in an asp410-to-tyr (D410Y) substitution, and another mutation in TRIP11. In patient 3, the second mutation was a 4-bp deletion in exon 13 (c.4815_4818delAGAG; 604505.0009), causing a frameshift predicted to result in a premature termination codon (Glu1606LeufsTer3), whereas in patient 5, it was a 2-bp deletion in exon 11 (c.2128_2129delAT; 604505.0010), also causing a frameshift predicted to result in a premature termination codon (Ile710CysfsTer19). Analysis of the c.1228G-T mutation for an effect on splicing revealed that it causes in-frame skipping of exon 9, resulting in a shortened protein (Asp410_Lys438del; designated GMAP207). Analysis of fibroblasts from patient 3 showed that 25% of mRNA contained exon 9, indicating that the aberrant splicing was not fully penetrant. Western blot of whole-cell lysates from patient 3 fibroblasts demonstrated a 3-kD lower GMAP207 protein, bearing the exon 9 missplice and a compound TRIP11 nonsense mutation; the mutant protein was present at levels only 10% of those of wildtype GMAP in controls. In addition, the missplicing associated with the c.1228G-T mutation was shown to be cell type-dependent, with a different splicing pattern in leukocytes: analysis of cDNA from white blood cells of patient 5 showed skipping of exons 8 and 9, causing a frameshift resulting in a premature termination codon (Asp410GlyfsTer12). Overexpression of the GMAP207 variant restored normal Golgi organization in GMAP210-deficient cells, consistent with some residual function. Mutant fibroblast-induced chondrocytes formed significantly fewer and smaller chondrogenic nodules, indicating that the production of bulk glycosylated proteoglycans was disrupted.
For discussion of the 4-bp deletion (c.4815_4818delAGAG, NM_004239.3) in exon 13 of the TRIP11 gene, causing a frameshift predicted to result in a premature termination codon (Glu1606LeufsTer3), that was found in compound heterozygous state in a 17-year-old Turkish girl (patient 3) with odontochondrodysplasia (ODCD1; 184260) by Wehrle et al. (2019), see 604505.0008.
Odontochondrodysplasia 1
For discussion of the 2-bp deletion (c.2128_2129delAT, NM_004239.3) in exon 11 of the TRIP11 gene, causing a frameshift predicted to result in a premature termination codon (Ile710CysfsTer19), that was found in compound heterozygous state in a 17-year-old Turkish girl (patient 5) with odontochondrodysplasia (ODCD1; 184260) by Wehrle et al. (2019), see 604505.0008.
Achondrogenesis, Type IA
In a male infant, born of nonconsanguineous Colombian parents, with achondrogenesis type IA (ACG1A; 200600), Vanegas et al. (2018) identified compound heterozygous frameshift mutations in exon 11 of the TRIP11 gene: a 2-bp deletion (c.2128_2129delAT), resulting in a frameshift and a premature termination codon (Ile710CysfsTer19), and a 4-bp deletion (c.2304_2307delTCAA; 604505.0013), resulting in a frameshift and a premature termination codon (Asn768LysfsTer7). The mutations, which were found by whole-exome sequencing and confirmed by Sanger sequencing, segregated with the phenotype in the family.
In a 12-year-old German boy (patient 6) with severe odontochondrodysplasia (ODCD1; 184260), Wehrle et al. (2019) identified compound heterozygosity for a 1-bp deletion (c.1622delA, NM_004239.3) in exon 11 of the TRIP11 gene, causing a frameshift predicted to result in a premature termination codon (Lys541ArgfsTer17), and a c.5416A-G transition in exon 18, predicted to result in a met1806-to-val (M1806V; 604505.0012) substitution. The authors analyzed the c.5416A-G mutation for an effect on splicing and observed exonic missplicing of exon 18, causing a frameshift resulting in a premature termination codon (Leu1805CysfsTer13); however, quantitative analysis also showed the presence of the M1806V substitution in 56% of cDNA transcripts. Immunofluorescence microscopy showed less intense GMAP staining in the patient than in controls, but RGB profile plots demonstrated that the residual protein was still correctly targeted to the cis-Golgi. However, there was compaction of the Golgi apparatus, and levels of pro-COL1A1 (120150) secreted by patient fibroblasts were significantly reduced compared to controls. In addition, mutant fibroblast-induced chondrocytes formed significantly fewer and smaller chondrogenic nodules, indicating that the production of bulk glycosylated proteoglycans was disrupted.
For discussion of the c.5416A-G transition in exon 18 of the TRIP11 gene, predicted to result in a met1806-to-val (M1806V; 604505.0012) substitution, but also shown to cause a frameshift resulting in a premature termination codon (Leu1805CysfsTer13), that was found in compound heterozygous state in a 12-year-old German boy (patient 6) with severe odontochondrodysplasia (ODCD1; 184260) by Wehrle et al. (2019), see 604505.0011.
For discussion of the 4-bp deletion (c.2304_2307delTCAA) in exon 11 of the TRIP11 gene, resulting in a frameshift and a premature termination codon (Asn768LysfsTer7), that was found in compound heterozygous state in a male infant with achondrogenesis type IA (ACG1A; 200600) by Vanegas et al. (2018), see 604505.0010.
Abe, A., Emi, N., Tanimoto, M., Terasaki, H., Marunouchi, T., Saito, H. Fusion of the platelet-derived growth factor receptor beta to a novel gene CEV14 in acute myelogenous leukemia after clonal evolution. Blood 90: 4271-4277, 1997. [PubMed: 9373237]
Chang, K.-H., Chen, Y., Chen, T.-T., Chou, W.-H., Chen, P.-L., Ma, Y.-Y., Yang-Feng, T. L., Leng, X., Tsai, M.-J., O'Malley, B. W., Lee, W.-H. A thyroid hormone receptor coactivator negatively regulated by the retinoblastoma protein. Proc. Nat. Acad. Sci. 94: 9040-9045, 1997. [PubMed: 9256431] [Full Text: https://doi.org/10.1073/pnas.94.17.9040]
Drin, G., Morello, V., Casella, J.-F., Gounon, P., Antonny, B. Asymmetric tethering of flat and curved lipid membranes by a golgin. Science 320: 670-673, 2008. [PubMed: 18451304] [Full Text: https://doi.org/10.1126/science.1155821]
Durfee, T., Becherer, K., Chen, P. L., Yeh, S. H., Yang, Y., Kilburn, A. E., Lee, W. H., Elledge, S. J. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. 7: 555-569, 1993. [PubMed: 8384581] [Full Text: https://doi.org/10.1101/gad.7.4.555]
Infante, C., Ramos-Morales, F., Fedriani, C., Bornens, M., Rios, R. M. GMAP-210, a cis-Golgi network-associated protein, is a minus end microtubule-binding protein. J. Cell Biol. 145: 83-98, 1999. Note: Erratum: J. Cell Biol. 158: 593 only, 2002. [PubMed: 10189370] [Full Text: https://doi.org/10.1083/jcb.145.1.83]
Lee, J. W., Choi, H.-S., Gyuris, J., Brent, R., Moore, D. D. Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Molec. Endocr. 9: 243-254, 1995. [PubMed: 7776974] [Full Text: https://doi.org/10.1210/mend.9.2.7776974]
Ramos-Morales, F., Vime, C., Bornens, M., Fedriani, C., Rios, R. M. Two splice variants of Golgi microtubule-associated protein of 210 kDa (GMAP-210) differ in their binding to the cis-Golgi network. Biochem. J. 357: 699-708, 2001. [PubMed: 11463340] [Full Text: https://doi.org/10.1042/0264-6021:3570699]
Rios, R. M., Sanchis, A., Tassin, A. M., Fedriani, C., Bornens, M. GMAP-210 recruits gamma-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation. Cell 118: 323-335, 2004. [PubMed: 15294158] [Full Text: https://doi.org/10.1016/j.cell.2004.07.012]
Smits, P., Bolton, A. D., Funari, V., Hong, M., Boyden, E. D., Lu, L., Manning, D. K., Dwyer, N. D., Moran, J. L., Prysak, M., Merriman, B., Nelson, S. F., Bonafe, L., Superti-Furga, A., Ikegawa, S., Krakow, D., Cohn, D. H., Kirchhausen, T., Warman, M. L., Beier, D. R. Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-210. New Eng. J. Med. 362: 206-216, 2010. [PubMed: 20089971] [Full Text: https://doi.org/10.1056/NEJMoa0900158]
Vanegas, S., Sua, L. F., Lopez-Tenorio, J., Ramirez-Montano, D., Pachajoa, H. Achondrogenesis type IA: clinical, histologic, molecular, and prenatal ultrasound diagnosis. Appl. Clin. Genet. 11: 69-73, 2018. [PubMed: 29872333] [Full Text: https://doi.org/10.2147/TACG.S157235]
Wehrle, A., Witkos, T. M., Unger, S., Schneider, J., Follit, J. A., Hermann, J., Welting, T., Fano, V., Hietala, M., Vatanavicharn, N. Schoner, K., Spranger, J. Schmidts, M., Zabel, B., Pazour, G. J., Bloch-Zupan, A., Nishimura, G., Superti-Furga, A., Lowe, M., Lausch, E. Hypomorphic mutations of TRIP11 cause odontochondrodysplasia. JCI Insight 4: 124701, 2019. Note: Electronic Article. [PubMed: 30728324] [Full Text: https://doi.org/10.1172/jci.insight.124701]
Wong, M., Munro, S. The specificity of vesicle traffic to the Golgi is encoded in the golgin coiled-coil proteins. Science 346: 1256898, 2014. Note: Electronic Article. [PubMed: 25359980] [Full Text: https://doi.org/10.1126/science.1256898]