The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane

Chishti, Athar H.; Kim, Anthony C.; Marfatia, Shirin M.; Lutchman, Mohini; Hanspal, Manjit; Jindal, Hitesh K.; Liu, Shih Chun; Low, Philip S.; Rouleau, Guy A.; Mohandas, Narla; Chasis, Joel Anne; Conboy, John G.; Gascard, Philippe; Takakuwa, Yuichi; Huang, Shih‐Tsung; Benz, Edward J.; Bretscher, Anthony; Fehon, Richard G.; Gusella, James F.; Ramesh, Vijaya; Solomon, Frank; Marchesi, V.; Tsukita, Shöichiro; Tsukita, Sachiko; Arpin, Monique; Louvard, Daniel; Tonks, Nicholas K.; Anderson, James M.; Fanning, Alan S.; Bryant, Peter J.; Woods, Daniel F.; Hoover, Kevin B.

doi:10.1016/s0968-0004(98)01237-7

Cited by 481 publications

(315 citation statements)

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“…3). Six of the myosins contain the myosin tail homology (MyTH4) [Chen et al, 1996] and/or ezrin, radixin, moesin homology (FERM) motifs [Chishti et al, 1998]. One myosin contains only MyTH4 in the tail domain, and one myosin contains only FERM.…”

Section: Myosin Genes Encode Divergent Unconventional Myosins In Tetrmentioning

confidence: 99%

Myosin genes in Tetrahymena

Williams

Gavin

2005

Cell Motil. Cytoskeleton

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Section: Myosin Genes Encode Divergent Unconventional Myosins In Tetrmentioning

confidence: 99%

Myosin genes in Tetrahymena

Williams

Gavin

2005

Cell Motil. Cytoskeleton

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“…These proteins also present other types of domains, including PDZ, tyrosine phosphatase, SH2-like, tyrosine kinase, kinase-like, myosin head, and PH domains [11]. In ERM proteins, the FERM domain is followed by a long α-helical region, which forms a coiled-coil structure, according to the only structure of full-length moesin available [12] (Fig 2A).…”

Section: General Overview Of Erm Proteins (Ezrin Radixin Moesin)mentioning

confidence: 99%

Model membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesin

2013

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Ezrin, radixin and moesin (ERM) proteins are now more and more recognized to play a key role in a large number of important physiological processes such as morphogenesis, cancer metastasis and virus infection. Several recent reviews extensively discuss their biological functions [1][2][3][4]. In this review, we will first remind the main features of this family of proteins, which are now known as linkers and regulators of the plasma membrane/cytoskeleton linkage. We will then briefly review their implication in pathological processes such as cancer and viral infection. In a second part, we will focus on biochemical and biophysical approaches to study ERM interaction with lipid membranes and conformational change in well-defined environments. In vitro studies using biomimetic lipid membranes, especially large unilamellar vesicles (LUVs), giant unilamellar vesicles (GUVs) and supported lipid bilayers (SLBs) and recombinant proteins help to understand the molecular mechanism of conformational activation of ERM proteins. These tools are aimed to decorticate the different steps of the interaction, to simplify the experiments performed in vivo in much more complex biological environments. KeywordsEzrin; radixin and moesin; biomimetic membranes; phosphoinositol (4,5)-bisphosphate (PIP 2 ); large unilamellar vesicles; supported lipid bilayers; giant unilamelar vesicles Corresponding author: Catherine Picart, CNRS UMR 5628 (LMGP), Grenoble Institute of Technology and CNRS, 3 parvis Louis Néel, F-38016 Grenoble Cedex, France. Europe PMC Funders GroupAuthor Manuscript Biochimie. Author manuscript; available in PMC 2014 July 28. Published in final edited form as:Biochimie. 2013 January ; 95(1): 3-11. doi:10.1016/j.biochi.2012.09.033. Europe PMC Funders Author ManuscriptsEurope PMC Funders Author Manuscripts Biological importance of Ezrin, Radixin and Moesin General overview of ERM proteins (Ezrin, Radixin, Moesin)ERM proteins are localized at the plasma membrane in actin-rich surface structures (Fig 1) [5], such as microvilli, membrane ruffles, and lamellipodia in gut cells, lymphocytes, hepatocytes, spermatozoids, fibroblasts and in a variety of other cell types [5][6][7][8][9]. They are involved in various physiological processes including establishment of cell polarity, cell motility and cell signaling [10]. They act as linkers between the plasma membrane and the cortical actin cytoskeleton. From a structural point of view, ERMs are constituted of 3 domains : a membrane binding domain, also known as FERM (for band 4.1 protein, ezrin, radixin and moesin), and intermediary region and a actin binding domain called C-ERMAD (for C-terminal ERM-association domain) (Fig 2A).The FERM domain, constituted of ~300 amino acids, is characteristic of the proteins of the band 4.1 superfamily. These proteins also present other types of domains, including PDZ, tyrosine phosphatase, SH2-like, tyrosine kinase, kinase-like, myosin head, and PH domains [11]. In ERM proteins, the FERM domain is followed by a long α-helical region, whi...

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“…Like the ERM proteins, merlin consists of three predicted structural domains [5,6,9]. The N-terminal domain, termed FERM (F for 4.1) domain, is highly conserved among all members of the ERM family and important for interactions with cell surface glycoproteins, including CD44 and intercellular adhesion molecules [10][11][12][13]. The second half of the molecule contains a predicted a-helical domain, which is also present in the ERM proteins.…”

Section: Caenorhabditis Elegansmentioning

confidence: 99%

The Role of Drosophila Merlin in the Control of Mitosis Exit and Development

Chang¹

2006

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Pu reporting burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the dal, needed, and completing and reviewing this collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, Including suggestions for reducing this4urden to Department of Defense, Washington Headquarters Services, Directorate for Information Operations and Reports (0704-0188), 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202-41o2. Respondents should be aware that notwithstanding any other provision of law, no person shall be subject to any penalty for failing to comply with a collection of information if it does not display a currently valid 0MB control number. PLEASE DO NOT RETURN YOUR FORM TO THE ABOVE ADDRESS. REPORT DATE (DD-MM-YYYY)2. REPORT SPONSORING / MONITORING AGENCY NAME(S) AND ADDRESS(ES) 10. SPONSOR/MONITOR'S ACRONYM(S) U.S. Army Medical Research and Materiel Command FortDetrick, Maryland 21702-5012 SPONSOR/MONITOR'S REPORT NUMBER(S)12. DISTRIBUTION / AVAILABILITY STATEMENT Approved for Public Release; Distribution Unlimited SUPPLEMENTARY NOTES14. ABSTRACT: Merlin, the NF2 gene product, shares a substantial homology with the ezrin-radixin-moesin (ERM) proteins. The merlin and ERM proteins are thought to be key regulators of interactions between the actin cytoskeleton and the plasma membrane in Schwann cells and polarized cells. They act as important members of signal transduction pathways that control cell growth and participate in the sorting of membrane proteins during exocytic traffic. Unlike ERM. Merlin has a distinct function as a tumor suppressor; however, the mechanism by which marline functions as a tumor suppressor is poorly understood. Drosophila melanogaster provides a genetic and developmental system that is amenable to experiment manipulation and has been very valuable to the study of tumor genetics. The Drosophila homolog of merlin shares sequence and functional similarity to the human protein. We have shown that merlin plays an important role in the control of mitosis exit and in the determination of dorsal/ventral compartment border during wing Imaginal disc development. Although merlin mutation did not seem to significantly affect the overall cell-cycle duration, merlin mutant displayed prolonged proliferation during the cell cycle. We showed that merlin is required for the determination of the wing morphology, and demonstrated a genetic interaction between merlin and porcupine, which controls the acetylation of the Wingless morphogen during the development of the wing imaginal disc. In addition, we showed a potential interaction between merlin and shibire, which is involved in wingless protein trafficking during early embryogenesis. Also, we found a role for merlin in spermatogenesis. Finally, we analyzed the origin and evolution of merlin, and identified a monophyletic origin of the merlin prot...

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The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane

Cited by 481 publications

References 35 publications

Myosin genes in Tetrahymena

Myosin genes in Tetrahymena

Model membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesin

The Role of Drosophila Merlin in the Control of Mitosis Exit and Development

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