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PMID:11089974

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Citation

Holmberg, J, Clarke, DL and Frisén, J (2000) Regulation of repulsion versus adhesion by different splice forms of an Eph receptor. Nature 408:203-6

Abstract

Eph tyrosine kinase receptors and their membrane-bound ephrin ligands mediate cell interactions and participate in several developmental processes. Ligand binding to an Eph receptor results in tyrosine phosphorylation of the kinase domain, and repulsion of axonal growth cones and migrating cells. Here we report that a subpopulation of ephrin-A5 null mice display neural tube defects resembling anencephaly in man. This is caused by the failure of the neural folds to fuse in the dorsal midline, suggesting that ephrin-A5, in addition to its involvement in cell repulsion, can participate in cell adhesion. During neurulation, ephrin-A5 is co-expressed with its cognate receptor EphA7 in cells at the edges of the dorsal neural folds. Three different EphA7 splice variants, a full-length form and two truncated versions lacking kinase domains, are expressed in the neural folds. Co-expression of an endogenously expressed truncated form of EphA7 suppresses tyrosine phosphorylation of the full-length EphA7 receptor and shifts the cellular response from repulsion to adhesion in vitro. We conclude that alternative usage of different splice forms of a tyrosine kinase receptor can mediate cellular adhesion or repulsion during embryonic development.

Links

PubMed Online version:10.1038/35041577

Keywords

Alternative Splicing; Animals; Cell Adhesion/physiology; Cell Line; Embryonic and Fetal Development/physiology; Ephrin-A5; Female; Male; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/physiology; Mice; Mutation; Nervous System/embryology; Neural Tube Defects/etiology; Neural Tube Defects/genetics; Neurons/cytology; Phosphorylation; Receptor Protein-Tyrosine Kinases/chemistry; Receptor Protein-Tyrosine Kinases/genetics; Receptor Protein-Tyrosine Kinases/physiology; Receptor, EphA7; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Signal Transduction

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

MOUSE:EFNA5

involved_in

GO:0022407: regulation of cell-cell adhesion

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:EFNA5

enables

GO:0046875: ephrin receptor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q61772

F

Seeded From UniProt

complete

MOUSE:EPHA7

involved_in

GO:0048013: ephrin receptor signaling pathway

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:EPHA7

involved_in

GO:0050730: regulation of peptidyl-tyrosine phosphorylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:EPHA7

involved_in

GO:0022407: regulation of cell-cell adhesion

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:EPHA7

enables

GO:0005004: GPI-linked ephrin receptor activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

MOUSE:EPHA7

involved_in

GO:0031952: regulation of protein autophosphorylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:EPHA7

located_in

GO:0005887: integral component of plasma membrane

ECO:0000305: curator inference used in manual assertion

GO:0005004

C

Seeded From UniProt

complete

MOUSE:EPHA7

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:O08543

F

Seeded From UniProt

complete


See also

References

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