Different properties of two isoforms of annexin XIII in MDCK cells

Autor: Frank Lafont, Paul Verkade, Sandra Lecat, Kai Simons, Klaus Fiedler, Christoph Thiele
Přispěvatelé: Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG), Max-Planck-Gesellschaft, Lecat, Sandra
Rok vydání: 2000
Předmět:
MESH: Amino Acid Sequence
[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]
MESH: Protein Isoforms
Fatty Acids
Monounsaturated
MESH: Recombinant Proteins
MESH: Dogs
Annexin
Protein Isoforms
MESH: Animals
MESH: Annexins
Sequence Deletion
MESH: Exocytosis
0303 health sciences
biology
030302 biochemistry & molecular biology
MESH: Sequence Deletion
Recombinant Proteins
3. Good health
Cell biology
MESH: Fatty Acids
Monounsaturated
Vesicular stomatitis virus
MESH: Calcium
Protein Binding
Gene isoform
Annexins
G protein
MESH: Biological Transport
Molecular Sequence Data
Hemagglutinin (influenza)
chemistry.chemical_element
Calcium
Exocytosis
Cell Line
03 medical and health sciences
Dogs
[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]
Animals
MESH: Protein Binding
Amino Acid Sequence
030304 developmental biology
Myristoylation
MESH: Molecular Sequence Data
Cell Membrane
Biological Transport
Cell Biology
biology.organism_classification
MESH: Cell Line
chemistry
MESH: Protein Processing
Post-Translational
biology.protein
Protein Processing
Post-Translational
Annexin A2
MESH: Cell Membrane
Zdroj: Journal of Cell Science
Journal of Cell Science, Company of Biologists, 2000, 113 ( Pt 14), pp.2607-18
Europe PubMed Central
ISSN: 1477-9137
0021-9533
DOI: 10.1242/jcs.113.14.2607
Popis: Annexins form a family of proteins that are widely expressed and known to bind membranes in the presence of calcium. Two isoforms of the annexin XIII subfamily are expressed in epithelia. We previously reported that annexin XIIIb is apically localized in MDCK cells and that it is involved in raft-mediated delivery of apical proteins. We have now analyzed the properties of annexin XIIIa, which differs from annexin XIIIb by a deletion of 41 amino acids in the amino-terminal domain, and is distributed both apically and basolaterally. Annexin XIIIa binding to membranes is independent of calcium but requires its myristoyl amino-terminal modification, as observed with annexin XIIIb. Our biochemical and functional data show that annexin XIIIa behaves differently in the apical and in the basolateral compartments. Whereas annexin XIIIa apically can associate with rafts independently of calcium, the basolateral pool requires calcium for this. Annexin XIIIa, like annexin XIIIb, stimulates apical transport of influenza virus hemagglutinin but, in contrast, only annexin XIIIa inhibits basolateral transport of vesicular stomatitis virus G protein. Our results suggest that annexin XIIIa and XIIIb have specific roles in epithelial cells, and because of their structural similarities, these isoforms offer interesting tools for unravelling the functions of annexins.
Databáze: OpenAIRE
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