The cytoplasmic tail of heparin-binding EGF-like growth factor regulates bidirectional intracellular trafficking between the plasma membrane and ER

FEBS Open Bio

Volumn 2, Issue , 2012, Pages 339-344

  Hieda, Miki ^a   Koizumi, Michiko ^a   Higashi, Chiduru ^a,c   Tachibana, Taro ^b   Taguchi, Tomohiko ^c   Higashiyama, Shigeki ^a  

^a EHIME UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b Osaka Prefecture University   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

Author keywords

Ectodomain shedding; ER retrieval; HB EGF; Intracellular trafficking

Indexed keywords

AMINO ACID; EPIDERMAL GROWTH FACTOR; HEPARIN;

ARTICLE; CELL MEMBRANE; CYTOPLASM; ENDOPLASMIC RETICULUM; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN MODIFICATION; RAT;

EID: 84867974986     PISSN: 22115463     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fob.2012.09.002     Document Type: Article

References (22)

1. Raab G., Klagsbrun M. Heparin-binding EGF-like growth factor. Biochim. Biophys. Acta. 1997, 1333:179-199.
2. Naglich J.G., Metherall J.E., Russell D.W., Eidels L. Expression cloning of a diphtheria toxin receptor: identity with a heparin-binding EGF-like growth factor precursor. Cell 1992, 69:1051-1061.
3. Higashiyama S., Abraham J.A., Miller J., Fiddes J.C., Klagsbrun M. A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF. Science 1991, 251:936-939.
4. Higashiyama S., Lau K., Besner G.E., Abraham J.A., Klagsbrun M. Structure of heparin-binding EGF-like growth factor. Multiple forms, primary structure, and glycosylation of the mature protein. J. Biol. Chem. 1992, 267. 6205-1622.
5. Goishi K., Higashiyama S., Klagsbrun M., Nakano N., Umata T., Ishikawa M., Mekada E., Taniguchi N. Phorbol ester induces the rapid processing of cell surface heparin-binding EGF-like growth factor: conversion from juxtacrine to paracrine growth factor activity. Mol. Biol. Cell 1995, 6:967-980.
6. Dethlefsen S.M., Raab G., Moses M.A., Adam R.M., Klagsbrun M., Freeman M.R. Extracellular calcium influx stimulates metalloproteinase cleavage and secretion of heparin-binding EGF-like growth factor independently of protein kinase C. J. Cell. Biochem. 1998, 69:143-153.
7. Prenzel N., Zwick E., Daub H., Leserer M., Abraham R., Wallasch C., Ullrich A. EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 1999, 402:884-888.
8. Hieda M., Isokane M., Koizumi M., Higashi C., Tachibana T., Shudou M., Tomohiko T., Hieda Y., Higashiyama S. Membrane-anchored growth factor, HB-EGF, on the cell surface targeted to the inner nuclear membrane. J. Cell Biol. 2008, 180:763-769.
9. Nanba D., Mammoto A., Hashimoto K., Higashiyama S. Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF. J. Cell Biol. 2003, 163:489-502.
10. Kinugasa Y., Hieda M., Hori M., Higashiyama S. The carboxyl-terminal fragment of proHB-EGF reversed Bcl6-mediated gene repression. J. Biol. Chem. 2007, 282:14797-14806.
11. Miyagawa J., Higashiyama S., Kawata S., Inui Y., Tamura S., Yamamoto K., Nishida M., Nakamura T., Yamashita S., Matsuzawa Y., Taniguchi N. Localization of heparin-binding EGF-like growth factor in the smooth muscle cells and macrophages of human atherosclerotic plaques. J. Clin. Invest. 1995, 95:404-411.
12. Misaki R., Nakagawa T., Fukuda M., Taniguchi N., Taguchi T. Spatial segregation of degradation- and recycling-trafficking pathways in COS-1 cells Biochem. Biophys. Res. Commun. 2007, 360:580-585.
13. Duden R. ER-to-Golgi transport: COP I and COP II function. Mol. Membr. Biol. 2003, 20:197-207.
14. Wang X., Mizushima H., Adachi S., Ohishi M., Iwamoto R., Mekada E. Cytoplasmic domain phosphorylation of heparin-binding EGF-like growth factor. Cell Struct. Funct. 2006, 31:15-27.
15. Hirata M., Umata T., Takahashi T., Ohnuma M., Miura Y., Iwamoto R., Mekada E. Identification of serum factor inducing ectodomain shedding of proHB-EGF and Studies of noncleavable mutants of proHB-EGF. Biochem. Biophys. Res. Commun. 2001, 283:915-922.
16. 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. 1999, 112:1149-1158.
17. Zito E., Buono M., Pepe S., Settembre C., Annunziata I., Surace EM., Dierks T., Monti M., Cozzolino M., Pucci P., Ballabio A., Cosma M.P. Sulfatase modifying factor 1 trafficking through the cells: from endoplasmic reticulum to the endoplasmic reticulum. EMBO J. 2007, 26:2443-2453.
18. Chen Y., Sánchez A., Rubio M.E., Kohl T., Pardo L.A., Stühmer W. Functional K(v)10.1 channels localize to the inner nuclear membrane. PLoS One 2011, 6:e19257.
19. Benlimame N., Le P.U., Nabi I.R. Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum. Mol. Biol. Cell 1998, 9. 1773-178.
20. Lamaze C., Jahannes L. Intracellular trafficking of bacterial and plant toxins. Comprehensive sourcebook of bacterial protein toxins 2006, Academic Press, London. 3rd ed. J.E. Alouf, M.R. Popoff (Eds.).
21. Letourneur F., Hennecke S., Demolliere C., Cosson P. Steric masking of a dilysine endoplasmic reticulum retention motif during assembly of the human high affinity receptor for immunoglobulin E. J. Cell Biol. 1995, 129:971-978.
22. Scott D.B., Blanpied T.A., Ehlers M.D. Coordinated PKA and PKC phosphorylation suppresses RXR-mediated ER retention and regulates the surface delivery of NMDA receptors. Neuropharmacology 2003, 45:755-767.