Mucolipidosis II-related mutations inhibit the exit from the endoplasmic reticulum and proteolytic cleavage of GlcNAc-1-phosphotransferase precursor protein (GNPTAB).

De Pace, Raffaella; Coutinho, Maria Francisca; Koch-Nolte, Friedrich; Haag, Friedrich; Prata, Maria João; Alves, Sandra; Braulke, Thomas; Pohl, Sandra

De Pace, Raffaella; Coutinho, Maria Francisca; Koch-Nolte, Friedrich; Haag, Friedrich; Prata, Maria João; Alves, Sandra; Braulke, Thomas; Pohl, Sandra.

Affiliation

De Pace R; Section Biochemistry, Children's Hospital, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.

Hum Mutat ; 35(3): 368-76, 2014 Mar.

Article in En | MEDLINE | ID: mdl-24375680

Subject(s)

Abnormalities, Multiple/genetics; Endoplasmic Reticulum/metabolism; Mucolipidoses/genetics; Mutation, Missense; Transferases (Other Substituted Phosphate Groups)/genetics; Alleles; Animals; CHO Cells; Child; Child, Preschool; Cricetulus; Female; Gene Expression Regulation, Neoplastic; Genotype; HEK293 Cells; HeLa Cells; Humans; Male; Phenotype; Proteolysis; RNA, Messenger/genetics; RNA, Messenger/metabolism

Key words

GNPTAB; Golgi; lysosomal storage disorder; mannose 6-phosphate; site-1 protease

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Abnormalities, Multiple / Transferases (Other Substituted Phosphate Groups) / Mutation, Missense / Endoplasmic Reticulum / Mucolipidoses Limits: Animals / Child / Child, preschool / Female / Humans / Male Language: En Journal: Hum Mutat Journal subject: GENETICA MEDICA Year: 2014 Type: Article Affiliation country: Germany

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