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Temporal Association of the N- andO-Linked Glycosylation Events and Their Implication in the Polarized Sorting of Intestinal Brush Border Sucrase-Isomaltase, Aminopeptidase N, and Dipeptidyl…
- H. Naim, G. Joberty, M. Alfalah, R. Jacob
- Biology, ChemistryThe Journal of Biological Chemistry
- 18 June 1999
The results indicate that O-linked carbohydrates are at least a part of the sorting mechanism of pro-SI and DPPIV and that the sorting of ApN implicates neitherO-linked nor N-linked glycans and is driven most likely by carbohydrate-independent mechanisms.
A Novel Type of Detergent-resistant Membranes May Contribute to an Early Protein Sorting Event in Epithelial Cells*
It is demonstrated that the mild detergent Tween 20 is adequate to discriminate between apical and basolateral proteins during early stages in their biosynthesis, and suggests an early polarized sorting mechanism prior to maturation in the Golgi apparatus.
O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts
Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease.
Intestinal Dipeptidyl Peptidase IV Is Efficiently Sorted to the Apical Membrane through the Concerted Action of N- andO-Glycans as Well as Association with Lipid Microdomains*
The data indicate that both types of glycosylation are critical components of the apical sorting signal of DPPIV, and cholesterol is a more critical component in this context than sphingolipids.
Distinct Cytoskeletal Tracks Direct Individual Vesicle Populations to the Apical Membrane of Epithelial Cells
Neuropeptide Y (NPY) cleaving enzymes: Structural and functional homologues of dipeptidyl peptidase 4
Structural Determinants Required for Apical Sorting of an Intestinal Brush-border Membrane Protein*
- R. Jacob, M. Alfalah, J. Grünberg, M. Obendorf, H. Naim
- BiologyThe Journal of Biological Chemistry
- 3 March 2000
It is concluded that the recognition signal for apical sorting of pro-SI comprises O-glycosylation of the Ala37-Pro48 stretch and requires the presence of the membrane anchoring domain.
Both Cleavage Products of the mCLCA3 Protein Are Secreted Soluble Proteins*
- L. Mundhenk, M. Alfalah, R. Elble, B. Pauli, H. Naim, A. Gruber
- BiologyJournal of Biological Chemistry
- 6 October 2006
The results suggest that the two mCLCA3 cleavage products cannot form an anion channel on their own but may instead act as extracellular signaling molecules.
Compound heterozygous mutations affect protein folding and function in patients with congenital sucrase-isomaltase deficiency.
The effects of mutations in the sucrase domain of SIC1229Y and SIF1745C indicate the importance of a direct interaction between isomaltase and sucrose and the role of sucrose as an intermolecular chaperone in the intracellular transport of SI.