* 614138

TRAFFICKING PROTEIN PARTICLE COMPLEX, SUBUNIT 11; TRAPPC11


Alternative titles; symbols

CHROMOSOME 4 OPEN READING FRAME 41; C4ORF41


HGNC Approved Gene Symbol: TRAPPC11

Cytogenetic location: 4q35.1     Genomic coordinates (GRCh38): 4:183,659,293-183,713,589 (from NCBI)


Gene-Phenotype Relationships
Location Phenotype Phenotype
MIM number
Inheritance Phenotype
mapping key
4q35.1 Muscular dystrophy, limb-girdle, autosomal recessive 18 615356 AR 3

TEXT

Description

TRAPPC11 is a component of the TRAPP multisubunit tethering complex involved in intracellular vesicle trafficking (Scrivens et al., 2011).


Cloning and Expression

Using tandem affinity purification followed by SDS-PAGE and mass spectrometry to identify proteins that copurified with TRAPPC2 (300202) and TRAPPC2L (610970) from HEK293 cells, Scrivens et al. (2011) identified TRAPPC11. TRAPPC11 had an apparent molecular mass of 129 kD by SDS-PAGE.


Mapping

Hartz (2011) mapped the TRAPPC11 gene to chromosome 4q35.1 based on an alignment of the TRAPPC11 sequence (GenBank AK022778) with the genomic sequence (GRCh37).


Gene Function

Scrivens et al. (2011) found that depletion of TRAPPC11 in HeLa cells via interfering RNA resulted in partial disassembly of the TRAPP complex. There was also Golgi fragmentation into dispersed punctae and arrested anterograde trafficking, suggesting that TRAPPC11 is involved in an early trafficking event between the endoplasmic reticulum (ER) and Golgi.

Using small interfering RNA in HeLa cells, DeRossi et al. (2016) found that knockdown of TRAPPC11, but not other TRAPP subunits, resulted in accumulation of nonglycosylated TRAP-alpha (SSR1; 600868).


Molecular Genetics

By whole-exome sequencing combined with linkage analysis of a Syrian family with limb-girdle muscular dystrophy-18 (LGMDR18; 615356), previously designated LGMD2S, Bogershausen et al. (2013) identified a homozygous mutation in the TRAPPC11 gene (G980R; 614138.0001). The same technique revealed a different homozygous mutation in the TRAPPC11 gene (Ala372_Ser429del; 614138.0002) in affected members of 2 Hutterite families with a slightly different phenotype. The G980R mutation occurred in the gryzun domain, whereas the deletion occurred in the foie gras domain. The Syrian patients had childhood onset of progressive proximal muscle weakness resulting in impaired ambulation. The shoulder girdle muscles were less severely affected than the hip girdle muscles. Other features included hip dysplasia, scoliosis, and increased serum creatine kinase. Affected individuals from the Hutterite families had early-onset psychomotor delay and evidence of a hyperkinetic movement disorder characterized mainly by choreiform movements of the trunk, limbs, and head, although athetoid movements, tremor, and dystonic posturing were also noted. All had truncal ataxia resulting in gait instability, mild muscle weakness, and increased serum creatine kinase. Patient cells from both groups showed increased fragmentation of the Golgi apparatus and decreased amounts of the mutant proteins. Studies in yeast suggested that the mutant missense protein lost the ability to interact properly with other TRAPP proteins. Patient cells also showed altered protein transport along the secretory pathway, with a delayed exit from the Golgi and a defect in the formation and/or movement of late endosomes/lysosomes. The findings suggested that altered membrane trafficking is the underlying molecular mechanism of this disease spectrum.

In an 8-year-old Han Chinese girl with a variant of LGMD2S, Liang et al. (2015) identified compound heterozygous mutations in the TRAPPC11 gene (614138.0001 and 614138.0003). The mutations, which were found by targeted next-generation sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. In addition to muscular dystrophy, the patient had delayed psychomotor development with borderline cognitive function, infantile-onset cataracts, and hepatic steatosis. Liang et al. (2015) noted that the 'foie gras' (foigr) mutant zebrafish shows lipid accumulation in hepatocytes (see ANIMAL MODEL).

In 4 patients from 2 unrelated consanguineous Turkish families with a variant of LGMD2S, Koehler et al. (2017) identified a homozygous splice site mutation in the TRAPPC11 gene (614138.0004). The mutation was found by a combination of autozygosity mapping and whole-exome sequencing and was confirmed by Sanger sequencing. It segregated with the disorder in both families. Haplotype analysis suggested a founder effect.


Animal Model

DeRossi et al. (2016) stated that 'foie gras' (foigr) mutant zebrafish exhibit lipid accumulation in hepatocytes and have a viral DNA insertion in the trappc11 gene that results in a C-terminally truncated protein. They found that trappc11 mutant larvae also had a defect in motility. Using Western blot analysis, DeRossi et al. (2016) detected mutant trappc11 at an apparent molecular mass of 56 kD and wildtype trappc11 at 129 kD. Foigr hepatocytes had a significant defect in synthesis of lipid-linked oligosaccharides, blocking protein N-glycosylation and causing protein misfolding, with chronic activation of the unfolded protein response (UPR) in ER. The block in N-glycosylation caused compensatory upregulation of nearly all genes involved in N-glycosylation and chronically stressed UPR-activated genes involved in sterol metabolism. Trappc11 mutant hepatocytes also developed abnormal ER morphology, fragmentation of the Golgi complex, and retention of secretory cargo. DeRossi et al. (2016) proposed that TRAPPC11 may function as a scaffold for enzymes of protein N-glycosylation or as a cofactor for an enzyme in lipid-linked oligosaccharide synthesis.


ALLELIC VARIANTS ( 4 Selected Examples):

.0001 MUSCULAR DYSTROPHY, LIMB-GIRDLE, AUTOSOMAL RECESSIVE 18

TRAPPC11, GLY980ARG
  
RCV000054408

In affected members of a consanguineous Syrian family with autosomal recessive limb-girdle muscular dystrophy type 2S (LGMDR18; 615356), Bogershausen et al. (2013) identified a homozygous c.2938G-A transition in the TRAPPC11 gene, resulting in a gly980-to-arg (G980R) substitution at a highly conserved residue in the gryzun domain. The mutation was found by exome sequencing combined with linkage analysis and confirmed by Sanger sequencing, segregated with the disorder in the family, and was not found in several large control databases or in 100 Turkish controls. Studies of patient cells indicated an intracellular trafficking defect.

In an 8-year-old Han Chinese girl with a variant of LGMDR18, Liang et al. (2015) identified compound heterozygous mutations in the TRAPPC11 gene: G980R and a splice site mutation (c.661-1G-T; 614138.0003). The mutations, which were found by targeted next-generation sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. In addition to muscular dystrophy, the patient had delayed psychomotor development with borderline cognitive function, infantile-onset cataracts, and hepatic steatosis.

DeRossi et al. (2016) found that patient fibroblasts with the G980R mutation showed abnormal accumulation of lipid droplets.


.0002 MUSCULAR DYSTROPHY, LIMB-GIRDLE, AUTOSOMAL RECESSIVE 18

TRAPPC11, IVS12DS, G-A, +5
  
RCV000054409...

In affected members of 2 Hutterite families with myopathy, a hyperkinetic muscle disorder, and global developmental delay (see 615356), Bogershausen et al. (2013) identified a homozygous G-to-A transition in intron 12 of the TRAPPC11 gene (c.1287+5G-A), resulting in a splice site site mutation and the generation of 2 abnormal transcripts that contain a large deletion (Ala372_Ser429del) in the foie gras domain, and a truncated protein, respectively. The mutation, which was found by homozygosity mapping and whole-exome sequencing, segregated with the disorder. The mutation was found at a frequency of 7% in control Hutterite populations. Studies of patient cells indicated an intracellular trafficking defect.


.0003 MUSCULAR DYSTROPHY, LIMB-GIRDLE, AUTOSOMAL RECESSIVE 18

TRAPPC11, IVS6AS, G-T, -1
  
RCV000258796

In an 8-year-old Han Chinese girl with a variant of limb-girdle muscular dystrophy type 2S (LGMDR18; 615356), Liang et al. (2015) identified compound heterozygous mutations in the TRAPPC11 gene: a G-to-T transversion in intron 6 (c.661-1G-T, NM_021942.5), resulting in a splice site alteration and the generation of 2 mutant transcripts predicted to result in truncated proteins (Leu240AlafsTer10 and Leu240ValfsTer7), and G980R (614138.0001). Patient muscle biopsy showed absence of the normal full-length TRAPPC11 protein. The mutations, which were found by targeted next-generation sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. In addition to muscular dystrophy, the patient had delayed psychomotor development with borderline cognitive function, infantile-onset cataracts, and hepatic steatosis.


.0004 MUSCULAR DYSTROPHY, LIMB-GIRDLE, AUTOSOMAL RECESSIVE 18

TRAPPC11, IVS18DS, A-G, +3
  
RCV000258806

In 4 patients from 2 unrelated consanguineous Turkish families with a variant of limb-girdle muscular dystrophy type 2S (LGMDR18; 615356), Koehler et al. (2017) identified a homozygous A-to-G transition in intron 18 of the TRAPPC11 gene (c.1893+3A-G, NM_021942.5), resulting in a splicing defect. The mutation was found by a combination of autozygosity mapping and whole-exome sequencing and was confirmed by Sanger sequencing. It segregated with the disorder in both families and was not found in the dbSNP, 1000 Genomes Project, or ExAC databases. Haplotype analysis suggested a founder effect. Analysis of patient cells showed that the mutation resulted in an aberrant out-of-frame transcript (Val588Glyfs16Ter) with only about 20% of the normal transcript compared to controls, and Western blot analysis showed a dramatic decrease in levels of the full-length protein. Patient cells showed hypoglycosylation of LAMP1 (153330). In vitro studies of patient fibroblasts showed that delayed exit through the Golgi apparatus of a marker protein, indicating a defect in secretory trafficking. In addition to muscular dystrophy, the patients had global developmental delay, intellectual disability with poor speech, alacrima, and achalasia.


REFERENCES

  1. Bogershausen, N., Shahrzad, N., Chong, J. X., von Kleist-Retzow, J.-C., Stanga, D., Li, Y., Bernier, F. P., Loucks, C. M., Wirth, R., Puffenberger, E. G., Hegele, R. A., Schreml, J., and 22 others. Recessive TRAPPC11 mutations cause a disease spectrum of limb girdle muscular dystrophy and myopathy with movement disorder and intellectual disability. Am. J. Hum. Genet. 93: 181-190, 2013. [PubMed: 23830518, images, related citations] [Full Text]

  2. DeRossi, C., Vacaru, A., Rafiq, R., Cinaroglu, A., Imrie, D., Nayar, S., Baryshnikova, A., Milev, M. P., Stanga, D., Kadakia, D., Gao, N., Chu, J., Freeze, H. H., Lehrman, M. A., Sacher, M., Sadler, K. C. trappc11 is required for protein glycosylation in zebrafish and humans. Molec. Biol. Cell 27: 1220-1234, 2016. [PubMed: 26912795, images, related citations] [Full Text]

  3. Hartz, P. A. Personal Communication. Baltimore, Md. 7/22/2011.

  4. Koehler, K., Milev, M. P., Prematilake, K., Reschke, F., Kutzner, S., Juhlen, R., Landgraf, D., Utine, E., Hazan, F., Diniz, G., Schuelke, M., Huebner, A., Sacher, M. A novel TRAPPC11 mutation in two Turkish families associated with cerebral atrophy, global retardation, scoliosis, achalasia and alacrima. J. Med. Genet. 54: 176-185, 2017. [PubMed: 27707803, related citations] [Full Text]

  5. Liang, W.-C., Zhu, W., Mitsuhashi, S., Noguchi, S., Sacher, M., Ogawa, M., Shih, H.-H., Jong, Y.-J., Nishino, I. Congenital muscular dystrophy with fatty liver and infantile-onset cataract caused by TRAPPC11 mutations: broadening of the phenotype. Skeletal Muscle 5: 29, 2015. Note: Electronic Article. [PubMed: 26322222, images, related citations] [Full Text]

  6. Scrivens, P. J., Noueihed, B., Shahrzad, N., Hul, S., Brunet, S., Sacher, M. C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking. Molec. Biol. Cell 22: 2083-2093, 2011. [PubMed: 21525244, images, related citations] [Full Text]


Cassandra L. Kniffin - updated : 11/04/2016
Patricia A. Hartz - updated : 11/03/2016
Cassandra L. Kniffin - updated : 8/1/2013
Creation Date:
Patricia A. Hartz : 8/4/2011
carol : 09/25/2018
carol : 02/21/2017
carol : 11/08/2016
ckniffin : 11/04/2016
mgross : 11/03/2016
mgross : 11/03/2016
carol : 08/02/2013
ckniffin : 8/1/2013
carol : 8/21/2012
wwang : 8/4/2011

* 614138

TRAFFICKING PROTEIN PARTICLE COMPLEX, SUBUNIT 11; TRAPPC11


Alternative titles; symbols

CHROMOSOME 4 OPEN READING FRAME 41; C4ORF41


HGNC Approved Gene Symbol: TRAPPC11

SNOMEDCT: 732929002;  


Cytogenetic location: 4q35.1     Genomic coordinates (GRCh38): 4:183,659,293-183,713,589 (from NCBI)


Gene-Phenotype Relationships

Location Phenotype Phenotype
MIM number
Inheritance Phenotype
mapping key
4q35.1 Muscular dystrophy, limb-girdle, autosomal recessive 18 615356 Autosomal recessive 3

TEXT

Description

TRAPPC11 is a component of the TRAPP multisubunit tethering complex involved in intracellular vesicle trafficking (Scrivens et al., 2011).


Cloning and Expression

Using tandem affinity purification followed by SDS-PAGE and mass spectrometry to identify proteins that copurified with TRAPPC2 (300202) and TRAPPC2L (610970) from HEK293 cells, Scrivens et al. (2011) identified TRAPPC11. TRAPPC11 had an apparent molecular mass of 129 kD by SDS-PAGE.


Mapping

Hartz (2011) mapped the TRAPPC11 gene to chromosome 4q35.1 based on an alignment of the TRAPPC11 sequence (GenBank AK022778) with the genomic sequence (GRCh37).


Gene Function

Scrivens et al. (2011) found that depletion of TRAPPC11 in HeLa cells via interfering RNA resulted in partial disassembly of the TRAPP complex. There was also Golgi fragmentation into dispersed punctae and arrested anterograde trafficking, suggesting that TRAPPC11 is involved in an early trafficking event between the endoplasmic reticulum (ER) and Golgi.

Using small interfering RNA in HeLa cells, DeRossi et al. (2016) found that knockdown of TRAPPC11, but not other TRAPP subunits, resulted in accumulation of nonglycosylated TRAP-alpha (SSR1; 600868).


Molecular Genetics

By whole-exome sequencing combined with linkage analysis of a Syrian family with limb-girdle muscular dystrophy-18 (LGMDR18; 615356), previously designated LGMD2S, Bogershausen et al. (2013) identified a homozygous mutation in the TRAPPC11 gene (G980R; 614138.0001). The same technique revealed a different homozygous mutation in the TRAPPC11 gene (Ala372_Ser429del; 614138.0002) in affected members of 2 Hutterite families with a slightly different phenotype. The G980R mutation occurred in the gryzun domain, whereas the deletion occurred in the foie gras domain. The Syrian patients had childhood onset of progressive proximal muscle weakness resulting in impaired ambulation. The shoulder girdle muscles were less severely affected than the hip girdle muscles. Other features included hip dysplasia, scoliosis, and increased serum creatine kinase. Affected individuals from the Hutterite families had early-onset psychomotor delay and evidence of a hyperkinetic movement disorder characterized mainly by choreiform movements of the trunk, limbs, and head, although athetoid movements, tremor, and dystonic posturing were also noted. All had truncal ataxia resulting in gait instability, mild muscle weakness, and increased serum creatine kinase. Patient cells from both groups showed increased fragmentation of the Golgi apparatus and decreased amounts of the mutant proteins. Studies in yeast suggested that the mutant missense protein lost the ability to interact properly with other TRAPP proteins. Patient cells also showed altered protein transport along the secretory pathway, with a delayed exit from the Golgi and a defect in the formation and/or movement of late endosomes/lysosomes. The findings suggested that altered membrane trafficking is the underlying molecular mechanism of this disease spectrum.

In an 8-year-old Han Chinese girl with a variant of LGMD2S, Liang et al. (2015) identified compound heterozygous mutations in the TRAPPC11 gene (614138.0001 and 614138.0003). The mutations, which were found by targeted next-generation sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. In addition to muscular dystrophy, the patient had delayed psychomotor development with borderline cognitive function, infantile-onset cataracts, and hepatic steatosis. Liang et al. (2015) noted that the 'foie gras' (foigr) mutant zebrafish shows lipid accumulation in hepatocytes (see ANIMAL MODEL).

In 4 patients from 2 unrelated consanguineous Turkish families with a variant of LGMD2S, Koehler et al. (2017) identified a homozygous splice site mutation in the TRAPPC11 gene (614138.0004). The mutation was found by a combination of autozygosity mapping and whole-exome sequencing and was confirmed by Sanger sequencing. It segregated with the disorder in both families. Haplotype analysis suggested a founder effect.


Animal Model

DeRossi et al. (2016) stated that 'foie gras' (foigr) mutant zebrafish exhibit lipid accumulation in hepatocytes and have a viral DNA insertion in the trappc11 gene that results in a C-terminally truncated protein. They found that trappc11 mutant larvae also had a defect in motility. Using Western blot analysis, DeRossi et al. (2016) detected mutant trappc11 at an apparent molecular mass of 56 kD and wildtype trappc11 at 129 kD. Foigr hepatocytes had a significant defect in synthesis of lipid-linked oligosaccharides, blocking protein N-glycosylation and causing protein misfolding, with chronic activation of the unfolded protein response (UPR) in ER. The block in N-glycosylation caused compensatory upregulation of nearly all genes involved in N-glycosylation and chronically stressed UPR-activated genes involved in sterol metabolism. Trappc11 mutant hepatocytes also developed abnormal ER morphology, fragmentation of the Golgi complex, and retention of secretory cargo. DeRossi et al. (2016) proposed that TRAPPC11 may function as a scaffold for enzymes of protein N-glycosylation or as a cofactor for an enzyme in lipid-linked oligosaccharide synthesis.


ALLELIC VARIANTS 4 Selected Examples):

.0001   MUSCULAR DYSTROPHY, LIMB-GIRDLE, AUTOSOMAL RECESSIVE 18

TRAPPC11, GLY980ARG
SNP: rs397509417, gnomAD: rs397509417, ClinVar: RCV000054408

In affected members of a consanguineous Syrian family with autosomal recessive limb-girdle muscular dystrophy type 2S (LGMDR18; 615356), Bogershausen et al. (2013) identified a homozygous c.2938G-A transition in the TRAPPC11 gene, resulting in a gly980-to-arg (G980R) substitution at a highly conserved residue in the gryzun domain. The mutation was found by exome sequencing combined with linkage analysis and confirmed by Sanger sequencing, segregated with the disorder in the family, and was not found in several large control databases or in 100 Turkish controls. Studies of patient cells indicated an intracellular trafficking defect.

In an 8-year-old Han Chinese girl with a variant of LGMDR18, Liang et al. (2015) identified compound heterozygous mutations in the TRAPPC11 gene: G980R and a splice site mutation (c.661-1G-T; 614138.0003). The mutations, which were found by targeted next-generation sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. In addition to muscular dystrophy, the patient had delayed psychomotor development with borderline cognitive function, infantile-onset cataracts, and hepatic steatosis.

DeRossi et al. (2016) found that patient fibroblasts with the G980R mutation showed abnormal accumulation of lipid droplets.


.0002   MUSCULAR DYSTROPHY, LIMB-GIRDLE, AUTOSOMAL RECESSIVE 18

TRAPPC11, IVS12DS, G-A, +5
SNP: rs397509418, gnomAD: rs397509418, ClinVar: RCV000054409, RCV000414573, RCV001254697

In affected members of 2 Hutterite families with myopathy, a hyperkinetic muscle disorder, and global developmental delay (see 615356), Bogershausen et al. (2013) identified a homozygous G-to-A transition in intron 12 of the TRAPPC11 gene (c.1287+5G-A), resulting in a splice site site mutation and the generation of 2 abnormal transcripts that contain a large deletion (Ala372_Ser429del) in the foie gras domain, and a truncated protein, respectively. The mutation, which was found by homozygosity mapping and whole-exome sequencing, segregated with the disorder. The mutation was found at a frequency of 7% in control Hutterite populations. Studies of patient cells indicated an intracellular trafficking defect.


.0003   MUSCULAR DYSTROPHY, LIMB-GIRDLE, AUTOSOMAL RECESSIVE 18

TRAPPC11, IVS6AS, G-T, -1
SNP: rs886041052, ClinVar: RCV000258796

In an 8-year-old Han Chinese girl with a variant of limb-girdle muscular dystrophy type 2S (LGMDR18; 615356), Liang et al. (2015) identified compound heterozygous mutations in the TRAPPC11 gene: a G-to-T transversion in intron 6 (c.661-1G-T, NM_021942.5), resulting in a splice site alteration and the generation of 2 mutant transcripts predicted to result in truncated proteins (Leu240AlafsTer10 and Leu240ValfsTer7), and G980R (614138.0001). Patient muscle biopsy showed absence of the normal full-length TRAPPC11 protein. The mutations, which were found by targeted next-generation sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. In addition to muscular dystrophy, the patient had delayed psychomotor development with borderline cognitive function, infantile-onset cataracts, and hepatic steatosis.


.0004   MUSCULAR DYSTROPHY, LIMB-GIRDLE, AUTOSOMAL RECESSIVE 18

TRAPPC11, IVS18DS, A-G, +3
SNP: rs886041053, ClinVar: RCV000258806

In 4 patients from 2 unrelated consanguineous Turkish families with a variant of limb-girdle muscular dystrophy type 2S (LGMDR18; 615356), Koehler et al. (2017) identified a homozygous A-to-G transition in intron 18 of the TRAPPC11 gene (c.1893+3A-G, NM_021942.5), resulting in a splicing defect. The mutation was found by a combination of autozygosity mapping and whole-exome sequencing and was confirmed by Sanger sequencing. It segregated with the disorder in both families and was not found in the dbSNP, 1000 Genomes Project, or ExAC databases. Haplotype analysis suggested a founder effect. Analysis of patient cells showed that the mutation resulted in an aberrant out-of-frame transcript (Val588Glyfs16Ter) with only about 20% of the normal transcript compared to controls, and Western blot analysis showed a dramatic decrease in levels of the full-length protein. Patient cells showed hypoglycosylation of LAMP1 (153330). In vitro studies of patient fibroblasts showed that delayed exit through the Golgi apparatus of a marker protein, indicating a defect in secretory trafficking. In addition to muscular dystrophy, the patients had global developmental delay, intellectual disability with poor speech, alacrima, and achalasia.


REFERENCES

  1. Bogershausen, N., Shahrzad, N., Chong, J. X., von Kleist-Retzow, J.-C., Stanga, D., Li, Y., Bernier, F. P., Loucks, C. M., Wirth, R., Puffenberger, E. G., Hegele, R. A., Schreml, J., and 22 others. Recessive TRAPPC11 mutations cause a disease spectrum of limb girdle muscular dystrophy and myopathy with movement disorder and intellectual disability. Am. J. Hum. Genet. 93: 181-190, 2013. [PubMed: 23830518] [Full Text: https://doi.org/10.1016/j.ajhg.2013.05.028]

  2. DeRossi, C., Vacaru, A., Rafiq, R., Cinaroglu, A., Imrie, D., Nayar, S., Baryshnikova, A., Milev, M. P., Stanga, D., Kadakia, D., Gao, N., Chu, J., Freeze, H. H., Lehrman, M. A., Sacher, M., Sadler, K. C. trappc11 is required for protein glycosylation in zebrafish and humans. Molec. Biol. Cell 27: 1220-1234, 2016. [PubMed: 26912795] [Full Text: https://doi.org/10.1091/mbc.E15-08-0557]

  3. Hartz, P. A. Personal Communication. Baltimore, Md. 7/22/2011.

  4. Koehler, K., Milev, M. P., Prematilake, K., Reschke, F., Kutzner, S., Juhlen, R., Landgraf, D., Utine, E., Hazan, F., Diniz, G., Schuelke, M., Huebner, A., Sacher, M. A novel TRAPPC11 mutation in two Turkish families associated with cerebral atrophy, global retardation, scoliosis, achalasia and alacrima. J. Med. Genet. 54: 176-185, 2017. [PubMed: 27707803] [Full Text: https://doi.org/10.1136/jmedgenet-2016-104108]

  5. Liang, W.-C., Zhu, W., Mitsuhashi, S., Noguchi, S., Sacher, M., Ogawa, M., Shih, H.-H., Jong, Y.-J., Nishino, I. Congenital muscular dystrophy with fatty liver and infantile-onset cataract caused by TRAPPC11 mutations: broadening of the phenotype. Skeletal Muscle 5: 29, 2015. Note: Electronic Article. [PubMed: 26322222] [Full Text: https://doi.org/10.1186/s13395-015-0056-4]

  6. Scrivens, P. J., Noueihed, B., Shahrzad, N., Hul, S., Brunet, S., Sacher, M. C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking. Molec. Biol. Cell 22: 2083-2093, 2011. [PubMed: 21525244] [Full Text: https://doi.org/10.1091/mbc.E10-11-0873]


Contributors:
Cassandra L. Kniffin - updated : 11/04/2016
Patricia A. Hartz - updated : 11/03/2016
Cassandra L. Kniffin - updated : 8/1/2013

Creation Date:
Patricia A. Hartz : 8/4/2011

Edit History:
carol : 09/25/2018
carol : 02/21/2017
carol : 11/08/2016
ckniffin : 11/04/2016
mgross : 11/03/2016
mgross : 11/03/2016
carol : 08/02/2013
ckniffin : 8/1/2013
carol : 8/21/2012
wwang : 8/4/2011