Figura, Kurt von

[["dc.bibliographiccitation.firstpage","2343"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","2350"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Pohlmann, Regina"],["dc.contributor.author","Krentler, Christiane"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Schröder, Wolfgang"],["dc.contributor.author","Lorkowski, Gerhard"],["dc.contributor.author","Culley, Jan"],["dc.contributor.author","Mersmann, Guenther"],["dc.contributor.author","Geier, Carola"],["dc.contributor.author","Waheed, Abdul"],["dc.contributor.author","Gottschalk, Stephen"],["dc.contributor.author","Grzeschik, Karl-Heinz"],["dc.contributor.author","Hasilik, Andrej"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:44Z"],["dc.date.available","2019-07-10T08:12:44Z"],["dc.date.issued","1988"],["dc.description.abstract","A 2112-bp cDNA clone (λCT29) encoding the entire sequence of the human lysosomal acid phosphatase (EC 3.1.3.2) was isolated from a λgt11 human placenta cDNA library. The cDNA hybridized with a 2.3-kb mRNA from human liver and HL-60 promyelocytes. The gene for lysosomal acid phosphatase was localized to human chromosome 11. The cDNA includes a 12-bp 5' noncoding region, an open reading frame of 1269 bp and an 831-bp 3' non-coding region with a putative polyadenylation signal 25 bp upstream of a 3' poly(A) tract. The deduced amino acid sequence reveals a putative signal sequence of 30 amino acids followed by a sequence of 393 amino acids that contains eight potential glycosylation sites and a hydrophobic region, which could function as a transmembrane domain. A 60% homology between the known 23 N-terminal amino acid residues of human prostatic acid phosphatase and the N-terminal sequence of lysosomal acid phosphatase suggests an evolutionary link between these two phosphatases. Insertion of the cDNA into the expression vector pSVL yielded a construct that encoded enzymatically active acid phosphatase in transfected monkey COS cells."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3431"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61020"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","lysosomal acid hydrolyase; human chromosome 11"],["dc.subject.ddc","610"],["dc.title","Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3497"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","3506"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Peters, Christoph"],["dc.contributor.author","Braun, Martin"],["dc.contributor.author","Weber, Birgit"],["dc.contributor.author","Wendland, Martin"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Pohlmann, Regina"],["dc.contributor.author","Waheed, Abdul"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:44Z"],["dc.date.available","2019-07-10T08:12:44Z"],["dc.date.issued","1990"],["dc.description.abstract","Lysosomal acid phosphatase (LAP) is synthesized as a transmembrane protein with a short carboxy-terminal cytoplasmic tail of 19 amino acids, and processed to a soluble protein after transport to lysosomes. Deletion of the membrane spanning domain and the cytoplasmic tail converts LAP to a secretory protein, while deletion of the cytoplasmic tail as well as substitution of tyrosine 413 within the cytoplasmic tail against phenylalanine causes accumulation at the cell surface. A chimeric polypeptide, in which the cytoplasmic tail of LAP was fused to the ectoplasmic and transmembrane domain of hemagglutinin is rapidly internalized and tyrosine 413 of the LAP tail is essential for internalization of the fusion protein. A chimeric polypeptide, in which the membrane spanning domain and cytoplasmic tail of LAP are fused to the ectoplasmic domain of the Mr 46 kd mannose 6-phosphate receptor, is rapidly transported to lysosomes, whereas wild type receptor is not transported to lysosomes. We conclude that a tyrosine containing endocytosis signal in the cytoplasmic tail of LAP is necessary and sufficient for targeting to lysosomes."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3435"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61024"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","endocytosis signal;intemalization; lysosomes; targeting"],["dc.subject.ddc","610"],["dc.title","Targeting of a lysosomal membrane protein: a tyrosine-containing endocytosis signal in the cytoplasmic tail of lysosomal acid phosphatase is necessary and sufficient for targeting to lysosomes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","18"],["dc.bibliographiccitation.journal","New England Journal of Medicine"],["dc.bibliographiccitation.lastpage","22"],["dc.bibliographiccitation.volume","324"],["dc.contributor.author","Polten, Andreas"],["dc.contributor.author","Fluharty, Arvan L."],["dc.contributor.author","Fluharty, Claire B."],["dc.contributor.author","Kappler, Joachim"],["dc.contributor.author","Figura, Kurt von"],["dc.contributor.author","Gieselmann, Volkmar"],["dc.date.accessioned","2019-07-10T08:12:45Z"],["dc.date.available","2019-07-10T08:12:45Z"],["dc.date.issued","1991"],["dc.description.abstract","Metachromatic leukodystrophy is an autosomal recessive inherited lysosomal storage disorder caused by a deficiency of arylsulfatase A. Three forms of the disease can be distinguished according to severity and the age at onset: late infantile (1 to 2 years), juvenile (3 to 16), and adult (> 16)."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3437"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61026"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Massachusetts Medical Society"],["dc.relation.issn","0028-4793"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","metachromatic leukodystrophy"],["dc.subject.ddc","610"],["dc.title","Molecular basis of different forms of metachromatic leukodystrophy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6816"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","6822"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Körner, Christian"],["dc.contributor.author","Knauer, Roland"],["dc.contributor.author","Stephani, Ulrich"],["dc.contributor.author","Marquardt, Thorsten"],["dc.contributor.author","Lehle, Ludwig"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:47Z"],["dc.date.available","2019-07-10T08:12:47Z"],["dc.date.issued","1999"],["dc.description.abstract","Type IV of the carbohydrate deficient glycoprotein syndromes (CDGp. is characterized by microcephaly, severe epilepsy, minimal psychomotor development and partial deficiency of sialic acids in serum glycoproteins. Here we show that the molecular defect in the index patient is a missense mutation in the gene encoding the mannosyltransferase that transfers mannose from dolichyl-phosphate mannose on to the lipid-linked oligosaccharide (LLO) intermediate Man5GlcNAc2-PP-dolichol. The defect results in the accumulation of the LLO intermediate and, due to its leaky nature, a residual formation of full-length LLOs. N-glycosylation is abnormal because of the transfer of truncated oligosaccharides in addition to that of full-length oligosaccharides and because of the incomplete utilization of N-glycosylation sites. The mannosyltransferase is the structural and functional orthologue of the Saccharomyces cerevisiae ALG3 gene."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3446"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61035"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","ALG3 gene; carbohydrate deficient glycoprotein syndrome"],["dc.subject.ddc","610"],["dc.title","Carbohydrate-deficient glycoprotein syndrome type IV: defieciency of dolichyl-P-Man:Man5GlcNAc2-PP-dolichyl mannosyltransferase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2084"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","2091"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Dierks, Thomas"],["dc.contributor.author","Lecca, M.Rita"],["dc.contributor.author","Schlotterhose, Petra"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:46Z"],["dc.date.available","2019-07-10T08:12:46Z"],["dc.date.issued","1999"],["dc.description.abstract","Sulfatases carry at their catalytic site a unique posttranslational modification, an a-formylglycine residue that is essential for enzyme activity. Formylglycine is generated by oxidation of a conserved cysteine or, in some prokaryotic sulfatases, serine residue. In eukaryotes, this oxidation occurs in the endoplasmic reticulum during or shortly after import of the nascent sulfatase polypeptide. The modification of arylsulfatase A was studied in vitro and was found to be directed by a short linear sequence, CTPSR, starting with the cysteine to be modified. Mutational analyses showed that the cysteine, proline and arginine are the key residues within this motif, whereas formylglycine formation tolerated the individual, but not the simultaneous substitution of the threonine or serine. The CTPp. motif was transferred to a heterologous protein leading to low-efficient formylglycine formation. The efficiency reached control values when seven additional residues (AALLTGR) directly following the CTPSR motif in arylsulfatase A were present. Mutating up to four residues simultaneously within this heptamer sequence inhibited the modification only moderately. AALLTGR may, therefore, have an auxiliary function in presenting the core motif to the modifying enzyme. Within the two motifs, the key residues are fully, and other residues are highly conserved among all known members of the sulfatase family."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3445"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61034"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","cysteine; endoplasmic reticulum; multiple sulfatase deficiency; protein modification; sulfatase"],["dc.subject.ddc","610"],["dc.title","Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1304"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","1314"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Höning, Stefan"],["dc.contributor.author","Sandoval, Ignacio V."],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:46Z"],["dc.date.available","2019-07-10T08:12:46Z"],["dc.date.issued","1998"],["dc.description.abstract","Among the various coats involved in vesicular transport, the clathrin associated coats that contain the adaptor complexes AP-1 and AP-2 are the most extensively characterized. The function of the recently described adaptor complex AP-3, which is similar to AP-1 and AP-2 in protein composition but does not associate with clathrin, is not known. By monitoring surface plasmon resonance we observed that AP-3 is able to interact with the tail of the lysosomal integral membrane protein LIMP-II and that this binding depends on a DEXXXLI sequence in the LIMP-II tail. Furthermore, AP-3 bound to the cytoplasmic tail of the melanosome-associated protein tyrosinase which contains a related EEXXXLL sequence. The tails of LIMP-II and tyrosinase either did not interact, or only interacted poorly, with AP-1 or AP-2. In contrast, the cytoplasmic tails of other membrane proteins containing di-leucine and/or tyrosine-based sorting signals did not bind AP-3, but AP-1 and/or AP-2. This points to a function of AP-3 in intracellular sorting to lysosomes and melanosomes of a subset of cargo proteins via di-leucine-based sorting motifs."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3443"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61032"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","biosensor; coated vesicles; endosome; membrane traffic; protein sorting"],["dc.subject.ddc","610"],["dc.title","A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","607"],["dc.bibliographiccitation.journal","The Journal of Pediatrics"],["dc.bibliographiccitation.lastpage","611"],["dc.bibliographiccitation.volume","83"],["dc.contributor.author","Figura, Kurt von"],["dc.contributor.author","Lögering, M."],["dc.contributor.author","Mersmann, G."],["dc.contributor.author","Kresse, H."],["dc.date.accessioned","2019-07-10T08:12:40Z"],["dc.date.available","2019-07-10T08:12:40Z"],["dc.date.issued","1973"],["dc.description.abstract","Three assays for the determination of N-acetyl-α- -D-glucosaminidase activity in the serum are described. In three families with patients suffering from Sanfilippo B disease, the affected individuals had a residual enzyme activity in the range of 2 to 16 per cent that of normal control subjects. Their obligate heterozygous parents had an activity diminished to 26 to 35 per cent. Nine other members of these families had enzyme activities lowered to the same extent and were therefore considered to be heterozygous carriers of the Sanfilippo B gene."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3256"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61001"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Elsevier"],["dc.relation.issn","0022-3476"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","serum assays; homozygous individuals; heterozygous individuals"],["dc.subject.ddc","610"],["dc.title","Sanfilippo B disease: Serum assays for detection of homozygous and heterozygous individuals in three families"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","761"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biochemical and Biophysical Research Communications"],["dc.bibliographiccitation.lastpage","767"],["dc.bibliographiccitation.volume","98"],["dc.contributor.author","Hasilik, A."],["dc.contributor.author","Waheed, A."],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:43Z"],["dc.date.available","2019-07-10T08:12:43Z"],["dc.date.issued","1981"],["dc.description.abstract","Summary: Recent finding of a-N-ocetylglucosamine( I)phospho(6)mannose diesters in lysosomal enzymes suggested that formation of monnose 6-phosphate residues involves transfer of N-acetylglucosamine l- hos hote to mannose. Using dephosphorylated R-hexosaminidase as acceptor and F t3-3 “I P UDP-N-acetylglucosamine OS donor for the phosphate group, phosphorylation of R-hexosaminidose by microsomes from rot liver, humon placenta and human skin fibroblosts wos achieved. The reaction was not affected by tunicomycin. Acid hydrolysis released monnose 6-[32P] phosphate from the phosphorylated l3-hexosaminidase. Our results suggest that lysosomal enzymes are phosphorylated by tronsfer of N-acetylglucosamine l-phosphate from UDP-N-ocetylglucosamine. The transferose activity wos deficient in fibroblasts from patients affected with l-cell disease. This deficiency is proposed to be the primary enzyme defect in I-ccl I disease."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3425"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61014"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Academic Press"],["dc.relation.issn","0006-291X"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","Enzymatic phosphorylation; lysosomal enzymes"],["dc.subject.ddc","610"],["dc.title","Enzymatic phosphorylation of lysosomal enzymes in the presence of UDP-N-acetylglucosamine. Absence of the activity in I-cell fibroblasts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2351"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","2358"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Waheed, Abdul"],["dc.contributor.author","Gottschalk, Stephen"],["dc.contributor.author","Hille, Annette"],["dc.contributor.author","Krentler, Christiane"],["dc.contributor.author","Pohlmann, Regina"],["dc.contributor.author","Braulke, Thomas"],["dc.contributor.author","Hauser, Hansjörg"],["dc.contributor.author","Geuze, Hans"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:44Z"],["dc.date.available","2019-07-10T08:12:44Z"],["dc.date.issued","1988"],["dc.description.abstract","BHK cells transfected with human lysosomal acid phosphatase (LAP) cDNA (CT29) expressed 70-fold higher enzyme activities of acid phosphatase than nontransfected BHK cells. The CT29-LAP was synthesized in BHK cells as a heterogeneously glycosylated precursor that was tightly membrane associated. Transfer to the trans-Golgi was associated with a small increase in size (~7 kd) and partial processing of the oligosaccharides to complex type structures. CT29-LAP was transferred into lysosomes as shown by subceliular fractionation, immunofluorescence and immunoelectron microscopy. Lack of mannose-6phosphate residues suggested that transport does not involve mannose-6phosphate receptors. Part of the membrane-associated CT29-LAP was processed to a soluble form. The mechanism that converts CT29-LAP into a soluble form was sensitive to NH4Cl, and reduced the size of the polypeptide by 7 kd. In vitro translation of CT29-derived cRNA in the presence of microsomal membranes yielded a CT29-LAP precursor that is protected from proteinase K except for a small peptide of -2 kd. In combination with the sequence data available for LAP, these observations suggest that CT29-LAP is synthesized and transported to lysosomes as a transmembrane protein. In the lysosomes, CT29-LAP is released from the membrane by proteolytic cleavage, which removes a C-terminal peptide including the transmembrane domain and the cytosolic tail of 18 amino acids."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3432"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61021"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","lysosomal membrane protein; protein transport"],["dc.subject.ddc","610"],["dc.title","Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes in transfected baby hamster kidney cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","73"],["dc.bibliographiccitation.journal","Nature Genetics"],["dc.bibliographiccitation.lastpage","76"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Lübke, Torben"],["dc.contributor.author","Marquardt, Thorsten"],["dc.contributor.author","Etzioni, Amos"],["dc.contributor.author","Hartmann, Enno"],["dc.contributor.author","Figura, Kurt von"],["dc.contributor.author","Körner, Christian"],["dc.date.accessioned","2019-07-09T11:52:20Z"],["dc.date.available","2019-07-09T11:52:20Z"],["dc.date.issued","2001"],["dc.description.abstract","Congenital disorders of glycosylation (CDG) comprise a rapidly growing group of inherited disorders in which glycosylation of glycoproteins is defective due to mutations in genes required for the assembly of lipid-linked oligosaccharides, their transfer to nascent glycoproteins (CDG-I) or the processing of protein-bound glycans1, 2 (CDG-II). Previously' a defect in the GDP-fucose import into the lumen of the Golgi was identified in a person with CDG (A.C.) with a general deficiency of fucosyl residues in glycoproteins3. This patient presents the clinical features of leukocyte adhesion deficiency type II (LAD II) including mental retardation, short stature, facial stigmata, and recurrent bacterial peripheral infections with persistently elevated peripheral leukocytes4, 5, 6, 7. Using a fucose-specific, lectin-staining procedure for detection of fucosylated glycoproteins and a retroviral cDNA library, we isolated a cDNA complementing the fucosylation defect in the patient's fibroblasts. The cDNA encodes a highly hydrophobic protein of 364 amino acids with multiple putative transmembrane domains. Restoration of GDP-fucose import activity in Golgi-enriched vesicles from the patient's fibroblasts verified the GDP-fucose transporter activity of this protein. We identified two missense mutations in the GDP-fucose transporter cDNA of patient A.C. and of two other people with LAD II. Thus complementation cloning allowed us to identify the human GDP-fucose transporter cDNA and GDP-fucose transporter deficiency as a cause for a new type of CDG. Following the recent recommendations2, 8 for the nomenclature for CDG, this new type is classified as CDG-IIc (formerly LAD II)."],["dc.identifier.doi","10.1038/ng0501-73"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3448"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60161"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1061-4036"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Complementation cloning identifies CDG-IIc, a new type of congenital disorders of glycosylation, as a GDP-fucose transporter deficiency"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]