The sucrase-isomaltase complex: Primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein
@article{Hunziker1986TheSC, title={The sucrase-isomaltase complex: Primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein}, author={Walter Hunziker and Martin Spiess and Giorgio Semenza and Harvey F. Lodish}, journal={Cell}, year={1986}, volume={46}, pages={227-234} }
249 Citations
Sucrase Is an Intramolecular Chaperone Located at the C-terminal End of the Sucrase-Isomaltase Enzyme Complex*
- Biology, ChemistryThe Journal of Biological Chemistry
- 2002
The interaction between SUC and the membrane-anchored IM leads to maturation of IM and blocks the secretion of SUC into the external milieu, concluding that SUC plays a role as an intramolecular chaperone in the context of the pro-SI protein.
Structure-function analysis of human sucrase-isomaltase identifies key residues required for catalytic activity
- Biology, ChemistryThe Journal of Biological Chemistry
- 2017
This approach provides a model for functional analysis of the single subunits within a multidomain protein, achieved without the necessity to express the individual subunits separately, and demonstrates that glucose product inhibition regulates the activities of both SI subunits.
The mode of anchoring and precursor forms of sucrase-isomaltase and maltase-glucoamylase in chicken intestinal brush-border membrane. Phylogenetic implications.
- Biology, ChemistryBiochimica et biophysica acta
- 1987
Molecular dissection of the NH2-terminal signal/anchor sequence of rat dipeptidyl peptidase IV
- Biology, ChemistryThe Journal of cell biology
- 1990
Structural features of the DPPIV amino-terminal signal-anchor sequences are discussed along with other types of sequences for their role in targeting nascent polypeptides to the RER.
Molecular Dissection of the NH 2-Terminal Signal / Anchor Sequence of Rat Dipeptidyl Peptidase IV
- Biology, Chemistry
- 2002
Site-directed mutagenesis studies show that deletion of this cytoplasmic domain does not affect translocation of nascent DPPIV polypeptide, but does affect significantly anchoring of the translocated polyPEptide in the microsomal membrane.
Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment.
- BiologyThe Journal of clinical investigation
- 1996
This is the first report that characterizes a point mutation in the SI gene that is responsible for the transport incompetence of SI and for its retention between the ER and the Golgi.
Primary structure and processing of the Candida tsukubaensisαāglucosidase
- Biology
- 1991
N-Terminal amino acid sequence analysis of the individual subunits of the purified enzyme, expressed in the recombinant host Saccharomyces cerevisiae, confirmed that the α-glucosidase precursor is proteolytically processed by removal of an N-terminal signal peptide to yield the two peptide subunits 1 and 2.
Additional N-Glycosylation and Its Impact on the Folding of Intestinal Lactase-phlorizin Hydrolase*
- BiologyThe Journal of Biological Chemistry
- 2000
The data strongly suggest that the LAC236 is implicated in the dimerization process of pro-LPH, most likely by nucleating the association of the ectodomains of the enzyme.
Characteristics and Structural Requirements of Apical Sorting of the Rat Growth Hormone through the O-Glycosylated Stalk Region of Intestinal Sucrase-isomaltase*
- BiologyThe Journal of Biological Chemistry
- 2001
The O-glycans in the stalk region of SI act as an apical sorting signal within a sorting machinery that comprises at least a carbohydrate-binding protein and fulfills specific spatial requirements provided, for example by a polyglycine spacer in the context of rGH or the P-domain within the SI enzyme complex.
A study of the molecular pathology of sucrase-isomaltase deficiency. A defect in the intracellular processing of the enzyme.
- BiologyThe New England journal of medicine
- 1987
Studies in a patient with primary sucrase-isomaltase deficiency demonstrated normal translation and high-mannose glycosylation of the precursor but a failure in further processing of the oligosaccharides, with subsequent intracellular degradation of the glycoprotein and undetectable enzymatic activity of intestinal sucrases.
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A simplified procedure for the isolation of the sucrase Ā· isomaltase complex from rabbit small intestine was worked out, which allows the preparation of this protein in a homogeneous form in goodā¦
Cellāfree synthesis of the oneāchain precursor of a major intrinsic protein complex of the smallāintestinal brush border membrane (proāsucraseāisomaltase)
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Hydrophobic labeling, isolation, and partial characterization of the NH2-terminal membranous segment of sucrase-isomaltase complex.
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