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A Recurrent De Novo Heterozygous COG4 Substitution Leads to Saul-Wilson Syndrome, Disrupted Vesicular Trafficking, and Altered Proteoglycan Glycosylation

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Harvard

Ferreira, CR, Xia, Z-J, Clément, A, Parry, DA, Davids, M, Taylan, F, Sharma, P, Turgeon, CT, Blanco-Sánchez, B, Ng, BG, Logan, CV, Wolfe, LA, Solomon, BD, Cho, MT, Douglas, G, Carvalho, DR, Bratke, H, Haug, MG, Phillips, JB, Wegner, J, Tiemeyer, M, Aoki, K, Nordgren, A, Hammarsjö, A, Duker, AL, Rohena, L, Hove, HB, Ek, J, Adams, D, Tifft, CJ, Onyekweli, T, Weixel, T, Macnamara, E, Radtke, K, Powis, Z, Earl, D, Gabriel, M, Russi, AHS, Brick, L, Kozenko, M, Tham, E, Raymond, KM, Phillips, JA, Tiller, GE, Wilson, WG, Hamid, R, Malicdan, MCV, Nishimura, G, Grigelioniene, G, Jackson, A & Undiagnosed Diseases Network 2018, 'A Recurrent De Novo Heterozygous COG4 Substitution Leads to Saul-Wilson Syndrome, Disrupted Vesicular Trafficking, and Altered Proteoglycan Glycosylation' American Journal of Human Genetics, vol. 103, no. 4, pp. 553-567. https://doi.org/10.1016/j.ajhg.2018.09.003

APA

CBE

Ferreira CR, Xia Z-J, Clément A, Parry DA, Davids M, Taylan F, Sharma P, Turgeon CT, Blanco-Sánchez B, Ng BG, Logan CV, Wolfe LA, Solomon BD, Cho MT, Douglas G, Carvalho DR, Bratke H, Haug MG, Phillips JB, Wegner J, Tiemeyer M, Aoki K, Nordgren A, Hammarsjö A, Duker AL, Rohena L, Hove HB, Ek J, Adams D, Tifft CJ, Onyekweli T, Weixel T, Macnamara E, Radtke K, Powis Z, Earl D, Gabriel M, Russi AHS, Brick L, Kozenko M, Tham E, Raymond KM, Phillips JA, Tiller GE, Wilson WG, Hamid R, Malicdan MCV, Nishimura G, Grigelioniene G, Jackson A, Undiagnosed Diseases Network. 2018. A Recurrent De Novo Heterozygous COG4 Substitution Leads to Saul-Wilson Syndrome, Disrupted Vesicular Trafficking, and Altered Proteoglycan Glycosylation. American Journal of Human Genetics. 103(4):553-567. https://doi.org/10.1016/j.ajhg.2018.09.003

MLA

Vancouver

Author

Ferreira, Carlos R ; Xia, Zhi-Jie ; Clément, Aurélie ; Parry, David A ; Davids, Mariska ; Taylan, Fulya ; Sharma, Prashant ; Turgeon, Coleman T ; Blanco-Sánchez, Bernardo ; Ng, Bobby G ; Logan, Clare V ; Wolfe, Lynne A ; Solomon, Benjamin D ; Cho, Megan T ; Douglas, Ganka ; Carvalho, Daniel R ; Bratke, Heiko ; Haug, Marte Gjøl ; Phillips, Jennifer B ; Wegner, Jeremy ; Tiemeyer, Michael ; Aoki, Kazuhiro ; Nordgren, Ann ; Hammarsjö, Anna ; Duker, Angela L ; Rohena, Luis ; Hove, Hanne Buciek ; Ek, Jakob ; Adams, David ; Tifft, Cynthia J ; Onyekweli, Tito ; Weixel, Tara ; Macnamara, Ellen ; Radtke, Kelly ; Powis, Zöe ; Earl, Dawn ; Gabriel, Melissa ; Russi, Alvaro H Serrano ; Brick, Lauren ; Kozenko, Mariya ; Tham, Emma ; Raymond, Kimiyo M ; Phillips, John A ; Tiller, George E ; Wilson, William G ; Hamid, Rizwan ; Malicdan, May C V ; Nishimura, Gen ; Grigelioniene, Giedre ; Jackson, Andrew ; Undiagnosed Diseases Network. / A Recurrent De Novo Heterozygous COG4 Substitution Leads to Saul-Wilson Syndrome, Disrupted Vesicular Trafficking, and Altered Proteoglycan Glycosylation. In: American Journal of Human Genetics. 2018 ; Vol. 103, No. 4. pp. 553-567.

Bibtex

@article{5ab716d8e8b140dbb40da5493614754c,
title = "A Recurrent De Novo Heterozygous COG4 Substitution Leads to Saul-Wilson Syndrome, Disrupted Vesicular Trafficking, and Altered Proteoglycan Glycosylation",
abstract = "The conserved oligomeric Golgi (COG) complex is involved in intracellular vesicular transport, and is composed of eight subunits distributed in two lobes, lobe A (COG1-4) and lobe B (COG5-8). We describe fourteen individuals with Saul-Wilson syndrome, a rare form of primordial dwarfism with characteristic facial and radiographic features. All affected subjects harbored heterozygous de novo variants in COG4, giving rise to the same recurrent amino acid substitution (p.Gly516Arg). Affected individuals' fibroblasts, whose COG4 mRNA and protein were not decreased, exhibited delayed anterograde vesicular trafficking from the ER to the Golgi and accelerated retrograde vesicular recycling from the Golgi to the ER. This altered steady-state equilibrium led to a decrease in Golgi volume, as well as morphologic abnormalities with collapse of the Golgi stacks. Despite these abnormalities of the Golgi apparatus, protein glycosylation in sera and fibroblasts from affected subjects was not notably altered, but decorin, a proteoglycan secreted into the extracellular matrix, showed altered Golgi-dependent glycosylation. In summary, we define a specific heterozygous COG4 substitution as the molecular basis of Saul-Wilson syndrome, a rare skeletal dysplasia distinct from biallelic COG4-CDG.",
author = "Ferreira, {Carlos R} and Zhi-Jie Xia and Aur{\'e}lie Cl{\'e}ment and Parry, {David A} and Mariska Davids and Fulya Taylan and Prashant Sharma and Turgeon, {Coleman T} and Bernardo Blanco-S{\'a}nchez and Ng, {Bobby G} and Logan, {Clare V} and Wolfe, {Lynne A} and Solomon, {Benjamin D} and Cho, {Megan T} and Ganka Douglas and Carvalho, {Daniel R} and Heiko Bratke and Haug, {Marte Gj{\o}l} and Phillips, {Jennifer B} and Jeremy Wegner and Michael Tiemeyer and Kazuhiro Aoki and Ann Nordgren and Anna Hammarsj{\"o} and Duker, {Angela L} and Luis Rohena and Hove, {Hanne Buciek} and Jakob Ek and David Adams and Tifft, {Cynthia J} and Tito Onyekweli and Tara Weixel and Ellen Macnamara and Kelly Radtke and Z{\"o}e Powis and Dawn Earl and Melissa Gabriel and Russi, {Alvaro H Serrano} and Lauren Brick and Mariya Kozenko and Emma Tham and Raymond, {Kimiyo M} and Phillips, {John A} and Tiller, {George E} and Wilson, {William G} and Rizwan Hamid and Malicdan, {May C V} and Gen Nishimura and Giedre Grigelioniene and Andrew Jackson and {Undiagnosed Diseases Network}",
note = "Published by Elsevier Inc.",
year = "2018",
month = "10",
day = "4",
doi = "10.1016/j.ajhg.2018.09.003",
language = "English",
volume = "103",
pages = "553--567",
journal = "American Journal of Human Genetics",
issn = "0002-9297",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - A Recurrent De Novo Heterozygous COG4 Substitution Leads to Saul-Wilson Syndrome, Disrupted Vesicular Trafficking, and Altered Proteoglycan Glycosylation

AU - Ferreira, Carlos R

AU - Xia, Zhi-Jie

AU - Clément, Aurélie

AU - Parry, David A

AU - Davids, Mariska

AU - Taylan, Fulya

AU - Sharma, Prashant

AU - Turgeon, Coleman T

AU - Blanco-Sánchez, Bernardo

AU - Ng, Bobby G

AU - Logan, Clare V

AU - Wolfe, Lynne A

AU - Solomon, Benjamin D

AU - Cho, Megan T

AU - Douglas, Ganka

AU - Carvalho, Daniel R

AU - Bratke, Heiko

AU - Haug, Marte Gjøl

AU - Phillips, Jennifer B

AU - Wegner, Jeremy

AU - Tiemeyer, Michael

AU - Aoki, Kazuhiro

AU - Nordgren, Ann

AU - Hammarsjö, Anna

AU - Duker, Angela L

AU - Rohena, Luis

AU - Hove, Hanne Buciek

AU - Ek, Jakob

AU - Adams, David

AU - Tifft, Cynthia J

AU - Onyekweli, Tito

AU - Weixel, Tara

AU - Macnamara, Ellen

AU - Radtke, Kelly

AU - Powis, Zöe

AU - Earl, Dawn

AU - Gabriel, Melissa

AU - Russi, Alvaro H Serrano

AU - Brick, Lauren

AU - Kozenko, Mariya

AU - Tham, Emma

AU - Raymond, Kimiyo M

AU - Phillips, John A

AU - Tiller, George E

AU - Wilson, William G

AU - Hamid, Rizwan

AU - Malicdan, May C V

AU - Nishimura, Gen

AU - Grigelioniene, Giedre

AU - Jackson, Andrew

AU - Undiagnosed Diseases Network

N1 - Published by Elsevier Inc.

PY - 2018/10/4

Y1 - 2018/10/4

N2 - The conserved oligomeric Golgi (COG) complex is involved in intracellular vesicular transport, and is composed of eight subunits distributed in two lobes, lobe A (COG1-4) and lobe B (COG5-8). We describe fourteen individuals with Saul-Wilson syndrome, a rare form of primordial dwarfism with characteristic facial and radiographic features. All affected subjects harbored heterozygous de novo variants in COG4, giving rise to the same recurrent amino acid substitution (p.Gly516Arg). Affected individuals' fibroblasts, whose COG4 mRNA and protein were not decreased, exhibited delayed anterograde vesicular trafficking from the ER to the Golgi and accelerated retrograde vesicular recycling from the Golgi to the ER. This altered steady-state equilibrium led to a decrease in Golgi volume, as well as morphologic abnormalities with collapse of the Golgi stacks. Despite these abnormalities of the Golgi apparatus, protein glycosylation in sera and fibroblasts from affected subjects was not notably altered, but decorin, a proteoglycan secreted into the extracellular matrix, showed altered Golgi-dependent glycosylation. In summary, we define a specific heterozygous COG4 substitution as the molecular basis of Saul-Wilson syndrome, a rare skeletal dysplasia distinct from biallelic COG4-CDG.

AB - The conserved oligomeric Golgi (COG) complex is involved in intracellular vesicular transport, and is composed of eight subunits distributed in two lobes, lobe A (COG1-4) and lobe B (COG5-8). We describe fourteen individuals with Saul-Wilson syndrome, a rare form of primordial dwarfism with characteristic facial and radiographic features. All affected subjects harbored heterozygous de novo variants in COG4, giving rise to the same recurrent amino acid substitution (p.Gly516Arg). Affected individuals' fibroblasts, whose COG4 mRNA and protein were not decreased, exhibited delayed anterograde vesicular trafficking from the ER to the Golgi and accelerated retrograde vesicular recycling from the Golgi to the ER. This altered steady-state equilibrium led to a decrease in Golgi volume, as well as morphologic abnormalities with collapse of the Golgi stacks. Despite these abnormalities of the Golgi apparatus, protein glycosylation in sera and fibroblasts from affected subjects was not notably altered, but decorin, a proteoglycan secreted into the extracellular matrix, showed altered Golgi-dependent glycosylation. In summary, we define a specific heterozygous COG4 substitution as the molecular basis of Saul-Wilson syndrome, a rare skeletal dysplasia distinct from biallelic COG4-CDG.

U2 - 10.1016/j.ajhg.2018.09.003

DO - 10.1016/j.ajhg.2018.09.003

M3 - Journal article

VL - 103

SP - 553

EP - 567

JO - American Journal of Human Genetics

JF - American Journal of Human Genetics

SN - 0002-9297

IS - 4

ER -

ID: 56073658