The tumour suppressor protein NF2/merlin: The puzzle continues

Journal of Clinical Neuroscience

Volumn 8, Issue 1, 2001, Pages 4-7

  Hovens, Christopher M ^a   Kaye, Andrew H ^a  

^a UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

Merlin; Neurofibromatosis type 2; Tumour suppressor

Indexed keywords

CALPAIN; MERLIN;

CARCINOGENESIS; GENETIC ANALYSIS; HUMAN; MOLECULAR CLONING; NEUROFIBROMATOSIS; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; REVIEW; TUMOR SUPPRESSOR GENE;

EID: 0035146734     PISSN: 09675868     EISSN: None     Source Type: Journal    
DOI: 10.1054/jocn.2000.0784     Document Type: Review

References (46)

1. Flanking markers bracket the neurofibromatosis type 2 (NF2) gene on chromosome 22
2. A genetic linkage map of the long arm of human chromosome 22
3. Common pathogenetic mechanism for three tumour types in bilateral acoustic neurofibromatosis
4. Alteration in a new gene encoding a putative membrane-organizing protein causes neurofibromatosis type 2
5. A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumour suppressor
6. Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures
7. ERM proteins: Head-to-tail regulation of actin-plasma membrane interaction
8. The ezrin protein family: Membrane-cytoskeleton interactions and disease associations
9. The FERM domain: A unique module involved in the linkage of cytoplasmic proteins to the membrane
10. Mutations in transcript isoforms of the neurofibromatosis 2 gene in multiple human tumour types
11. Novel alternatively spliced isoforms of the neurofibromatosis type 2 tumour suppressor are targeted to the nucleus and cytoplasmic granules
12. Merlin differentially associates with the microtubule and actin cytoskeleton
13. Endoplasmic reticulum localization of Sec 12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain
14. ICAM-2 redistributed by ezrin as a target for killer cells
15. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
16. Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization
17. Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2
18. Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4,5-bisphosphate
19. A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding
20. Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site
21. Homotypic and heterotypic interaction of the neurofibromatosis 2 tumour suppressor protein merlin and the ERM protein ezrin
22. Interdomain interaction of merlin isoforms and its influence on intermolecular binding to NHE-RF
23. Neurofibromatosis 2 tumour suppressor schwannomin interacts with betall-spectrin
24. NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins
25. Neurofibromatosis 2 tumor suppressor protein colocalizes with ezrin and CD44 and associates with actin-containing cytoskeleton
26. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
27. Rho regulates association of both the ERM family and vinculin with the plasma membrane in MDCK cells
28. RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
29. Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
30. Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures
31. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association
32. Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cells
33. The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein
34. Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor
35. Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin
36. Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway
37. Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members
38. Isolation of mutations in the Drosophila homologues of the human Neurofibromatosis 2 and yeast CDC42 genes using a simple and efficient reverse-genetic method
39. The Nf2 tumor suppressor gene product is essential for extraembryonic development immediately prior to gastrulation
40. Structural analysis of Drosophila merlin reveals functional domains important for growth control and subcellular localization
41. Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin
42. Interdomain binding mediates tumor growth suppression by the NF2 gene product
43. Universal absence of merlin, but not other ERM family members, in schwannomas
44. Mice heterozygous for a mutation at the Nf2 tumor suppressor locus develop a range of highly metastatic tumors
45. The involvement of calpain-dependent proteolysis of the tumor suppressor NF2 (merlin) in schwannomas and meningiomas
46. In vitro growth inhibition of growth factor-stimulated meningioma cells by calcium channel antagonists