Comparative study of ezrin phosphorylation among different tissues: More is good; too much is bad

American Journal of Physiology - Cell Physiology

Volumn 295, Issue 1, 2008, Pages

  Zhu, Lixin ^a   Hatakeyama, Jason ^a   Chen, Cheng ^a   Shastri, Aditi ^a   Poon, Kevin ^a   Forte, John G ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Intestine; Kidney; Membrane cytoskeleton; Phosphorylation; Stomach

Indexed keywords

EZRIN; F ACTIN; SODIUM AZIDE; STAUROSPORINE; ACTIN; CYTOSKELETON PROTEIN; THREONINE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; CYTOSKELETON; KIDNEY PROXIMAL TUBULE; NONHUMAN; PLASTICITY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; RABBIT; STOMACH GLAND; STOMACH PARIETAL CELL; ANIMAL; ANTIBODY SPECIFICITY; CELL MEMBRANE; CYTOLOGY; EPITHELIUM CELL; GENETICS; IN VITRO STUDY; INTESTINE CELL; INTESTINE MUCOSA; METABOLISM; MICROVILLUS; MUTATION; PHOSPHORYLATION; SMALL INTESTINE;

ACTINS; ANIMALS; CELL MEMBRANE; CYTOSKELETAL PROTEINS; CYTOSKELETON; ENTEROCYTES; EPITHELIAL CELLS; INTESTINAL MUCOSA; INTESTINE, SMALL; KIDNEY TUBULES, PROXIMAL; MICROVILLI; MUTATION; ORGAN SPECIFICITY; PHOSPHORYLATION; RABBITS; THREONINE;

EID: 52749086539     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00159.2008     Document Type: Article

References (49)

1. Algrain M, Turunen O, Vaheri A, Louvard D, Arpin M. Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J Cell Biol 120: 129-139, 1993.
2. Ammar DA, Nguyen PN, Forte JG. Functionally distinct pools of actin in secretory cells. Am J Physiol Cell Physiol 281: C407-C417, 2001.
3. Berryman M, Franck Z, Bretscher A. Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. J Cell Sci 105: 1025-1043, 1993.
4. Bretscher A. Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor. J Cell Biol 108: 921-930, 1989.
5. Bretscher A. Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr Opin Cell Biol 11: 109-116, 1999.
6. Bretscher A, Reczek D, Berryman M. Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J Cell Sci 110: 3011-3018, 1997.
7. Brown D, Lee R, Bonventre JV. Redistribution of villin to proximal tubule basolateral membranes after ischemia and reperfusion. Am J Physiol Renal Physiol 273: F1003-F1012, 1997.
8. Chen J, Cohn JA, Mandel LJ. Dephosphorylation of ezrin as an early event in renal microvillar breakdown and anoxic injury. Proc Natl Acad Sci USA 92: 7495-7499, 1995.
9. Chen J, Doctor RB, Mandel LJ. Cytoskeletal dissociation of ezrin during renal anoxia: role in microvillar injury. Am J Physiol Cell Physiol 267: C784-C795, 1994.
10. Chishti AH, Kim AC, Marfatia SM, Lutchman M, Hanspal M, Jindal H, Liu SC, Low PS, Rouleau GA, Mohandas N, Chasis JA, Conboy JG, Gascard P, Takakuwa Y, Huang SC, Benz EJ Jr, Bretscher A, Fehon RG, Gusella JF, Ramesh V, Solomon F, Marchesi VT, Tsukita S, Arpin M, Louvard D, Tonks NK, Anderson JM, Fanning AS, Bryant PJ, Woods DF, Hoover KB. The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane. Trends Biochem Sci 23: 281-282, 1998.
11. Dard N, Louvet-Vallee S, Santa-Maria A, Maro B. Phosphorylation of ezrin on threonine T567 plays a crucial role during compaction in the mouse early embryo. Dev Biol 271: 87-97, 2004.
12. Fievet BT, Gautreau A, Roy C, Del Maestro L, Mangeat P, Louvard D, Arpin M. Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin. J Cell Biol 164: 653-659, 2004.
13. Forte TM, Machen TE, Forte JG. Ultrastructural changes in oxyntic cells associated with secretory function: a membrane-recycling hypothesis. Gastroenterology 73: 941-955, 1977.
14. Gary R, Bretscher A. Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site. Mol Biol Cell 6: 1061-1075, 1995.
15. Gautreau A, Louvard D, Arpin M. Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane. J Cell Biol 150: 193-203, 2000.
16. Gonzalez-Agosti C, Wiederhold T, Herndon ME, Gusella J, Ramesh V. Interdomain interaction of merlin isoforms and its influence on intermolecular binding to NHE-RF. J Biol Chem 274: 34438-34442, 1999.
17. Gould KL, Bretscher A, Esch FS, Hunter T. cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1. EMBO J 8: 4133-4142, 1989.
18. Hanzel D, Reggio H, Bretscher A, Forte JG, Mangeat P. The secretion-stimulated 80K phosphoprotein of parietal cells is ezrin, and has properties of a membrane cytoskeletal linker in the induced apical microvilli. EMBO J 10: 2363-2373, 1991.
19. Hayashi K, Yonemura S, Matsui T, Tsukita S. Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues. J Cell Sci 112: 1149-1158, 1999.
20. Hishiya A, Ohnishi M, Tamura S, Nakamura F. Protein phosphatase 2C inactivates F-actin binding of human platelet moesin. J Biol Chem 274: 26705-26712, 1999.
21. Hoeflich KP, Tsukita S, Hicks L, Kay CM, Ikura M. Insights into a single rod-like helix in activated radixin required for membrane-cytoskeletal cross-linking. Biochemistry 42: 11634-11641, 2003.
22. i and changes in intracellular pH during chemical anoxia in mouse neocortical neurons in primary culture. J Neurosci Res 56: 358-370, 1999.
23. +-ATPase is induced by Rho small GTPase in renal epithelial cells. Biochem Biophys Res Commun 297: 1231-1237, 2002.
24. Malinowska DH, Koelz HR, Hersey SJ, Sachs G. Properties of the gastric proton pump in unstimulated permeable gastric glands. Proc Natl Acad Sci USA 78: 5908-5912, 1981.
25. Matsui T, Maeda M, Doi Y, Yonemura S, Amano M, Kaibuchi K, Tsukita S. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J Cell Biol 140: 647-657, 1998.
26. Molitoris BA. Ischemia-induced loss of epithelial polarity: potential role of the actin cytoskeleton. Am J Physiol Renal Fluid Electrolyte Physiol 260: F769-F778, 1991.
27. +-ATPase that redistributes to apical membrane during ATP depletion remains functional. Am J Physiol Renal Fluid Electrolyte Physiol 265: F693-F697, 1993.
28. +-ATPase during ischemia. Am J Physiol Renal Fluid Electrolyte Physiol 263: F488-F495, 1992.
29. Molitoris BA, Falk SA, Dahl RH. Ischemia-induced loss of epithelial polarity. Role of the tight junction. J Clin Invest 84: 1334-1339, 1989.
30. Nakamura F, Amieva MR, Furthmayr H. Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets. J Biol Chem 270: 31377-31385, 1995.
31. Nakamura F, Huang L, Pestonjamasp K, Luna EJ, Furthmayr H. Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides. Mol Biol Cell 10: 2669-2685, 1999.
32. Niggli V, Andreoli C, Roy C, Mangeat P. Identification of a phosphatidylinositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin. FEBS Lett 376: 172-176, 1995.
33. Oshiro N, Fukata Y, Kaibuchi K. Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures. J Biol Chem 273: 34663-34666, 1998.
34. Pearson MA, Reczek D, Bretscher A, Karplus PA. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 101: 259-270, 2000.
35. Schulz I. Permeabilizing cells: some methods and applications for the study of intracellular processes. Methods Enzymol 192: 280-300, 1990.
36. Shiue H, Musch MW, Wang Y, Chang EB, Turner JR. Akt2 phosphorylates ezrin to trigger NHE3 translocation and activation. J Biol Chem 280: 1688-1695, 2005.
37. Simons PC, Pietromonaco SF, Reczek D, Bretscher A, Elias L. C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton. Biochem Biophys Res Commun 253: 561-565, 1998.
38. Tamura A, Kikuchi S, Hata M, Katsuno T, Matsui T, Hayashi H, Suzuki Y, Noda T, Tsukita S. Achlorhydria by ezrin knockdown: defects in the formation/expansion of apical canaliculi in gastric parietal cells. J Cell Biol 169: 21-28, 2005.
39. Urushidani T, Hanzel DK, Forte JG. Characterization of an 80-kDa phosphoprotein involved in parietal cell stimulation. Am J Physiol Gastrointest Liver Physiol 256: G1070-G1081, 1989.
40. Urushidani T, Hanzel DK, Forte JG. Protein phosphorylation associated with stimulation of rabbit gastric glands. Biochim Biophys Acta 930: 209-219, 1987.
41. Varming T, Drejer J, Frandsen A, Schousboe A. Characterization of a chemical anoxia model in cerebellar granule neurons using sodium azide: protection by nifedipine and MK-801. J Neurosci Res 44: 40-46, 1996.
42. Wu YX, Uezato T, Fujita M. Tyrosine phosphorylation and cellular redistribution of ezrin in MDCK cells treated with pervanadate. J Cell Biochem 79: 311-321, 2000.
43. + Transport, edited by Hirst BH. Heidelberg, Germany: Springer-Verlag, 1994, p. 341-349.
44. Yonemura S, Matsui T, Tsukita S. Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo. J Cell Sci 115: 2569-2580, 2002.
45. Yonemura S, Tsukita S. Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins. J Cell Biol 145: 1497-1509, 1999.
46. Yoshinaga-Ohara N, Takahashi A, Uchiyama T, Sasada M. Spatio-temporal regulation of moesin phosphorylation and rear release by Rho and serine/threonine phosphatase during neutrophil migration. Exp Cell Res 278: 112-122, 2002.
47. Zhou R, Zhu L, Kodani A, Hauser P, Yao X, Forte JG. Phosphorylation of ezrin on threonine 567 produces a change in secretory phenotype and repolarizes the gastric parietal cell. J Cell Sci 118: 4381-4391, 2005.
48. Zhu L, Liu Y, Forte JG. Ezrin oligomers are the membrane-bound dormant form in gastric parietal cells. Am J Physiol Cell Physiol 288: C1242-C1254, 2005.
49. Zhu L, Zhou R, Mettler S, Wu T, Abbas A, Delaney J, Forte JG. High turnover of ezrin T567 phosphorylation: conformation, activity, and cellular function. Am J Physiol Cell Physiol 293: C874-C884, 2007.