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Volumn 2, Issue 2, 2016, Pages 131-157

Loss of MYO5B in Mice Recapitulates Microvillus Inclusion Disease and Reveals an Apical Trafficking Pathway Distinct to Neonatal Duodenum

Author keywords

Brush Border; Enterocyte Trafficking; MYO5B; NHE3; Rab11a; Rab8a; Syntaxin 3

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); COMMON ACUTE LYMPHOBLASTIC LEUKEMIA ANTIGEN; EZRIN; IMMUNOGLOBULIN G ANTIBODY; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; MESSENGER RNA; MYOSIN V; MYOSIN VB; PROTEIN P120; RAB PROTEIN; RAB11A PROTEIN; RAB8A PROTEIN; SNARE PROTEIN; SODIUM PROTON EXCHANGE PROTEIN 3; STX3 PROTEIN; TAMOXIFEN; UNCLASSIFIED DRUG; UVOMORULIN; VILLIN;

EID: 84975763782     PISSN: None     EISSN: 2352345X     Source Type: Journal    
DOI: 10.1016/j.jcmgh.2015.11.009     Document Type: Article
Times cited : (62)

References (37)
  • 1
    • 57149111944 scopus 로고    scopus 로고
    • Navajo microvillous inclusion disease is due to a mutation in MYO5B
    • Erickson R.P., Larson-Thome K., Valenzuela R.K., et al. Navajo microvillous inclusion disease is due to a mutation in MYO5B. Am J Med Genet A 2008, 146A:3117-3119.
    • (2008) Am J Med Genet A , vol.146A , pp. 3117-3119
    • Erickson, R.P.1    Larson-Thome, K.2    Valenzuela, R.K.3
  • 2
    • 52949112224 scopus 로고    scopus 로고
    • MYO5B mutations cause microvillus inclusion disease and disrupt epithelial cell polarity
    • Muller T., Hess M.W., Schiefermeier N., et al. MYO5B mutations cause microvillus inclusion disease and disrupt epithelial cell polarity. Nat Genet 2008, 40:1163-1165.
    • (2008) Nat Genet , vol.40 , pp. 1163-1165
    • Muller, T.1    Hess, M.W.2    Schiefermeier, N.3
  • 3
    • 77951857203 scopus 로고    scopus 로고
    • Loss-of-function of MYO5B is the main cause of microvillus inclusion disease: 15 novel mutations and a CaCo-2 RNAi cell model
    • Ruemmele F.M., Muller T., Schiefermeier N., et al. Loss-of-function of MYO5B is the main cause of microvillus inclusion disease: 15 novel mutations and a CaCo-2 RNAi cell model. Hum Mutat 2010, 31:544-551.
    • (2010) Hum Mutat , vol.31 , pp. 544-551
    • Ruemmele, F.M.1    Muller, T.2    Schiefermeier, N.3
  • 4
    • 0018178824 scopus 로고
    • Familial enteropathy: a syndrome of protracted diarrhea from birth, failure to thrive, and hypoplastic villus atrophy
    • Davidson G.P., Cutz E., Hamilton J.R., et al. Familial enteropathy: a syndrome of protracted diarrhea from birth, failure to thrive, and hypoplastic villus atrophy. Gastroenterology 1978, 75:783-790.
    • (1978) Gastroenterology , vol.75 , pp. 783-790
    • Davidson, G.P.1    Cutz, E.2    Hamilton, J.R.3
  • 6
    • 0033754550 scopus 로고    scopus 로고
    • Microvillus inclusion disease: a genetic defect affecting apical membrane protein traffic in intestinal epithelium
    • Ameen N.A., Salas P.J. Microvillus inclusion disease: a genetic defect affecting apical membrane protein traffic in intestinal epithelium. Traffic 2000, 1:76-83.
    • (2000) Traffic , vol.1 , pp. 76-83
    • Ameen, N.A.1    Salas, P.J.2
  • 7
    • 84922394222 scopus 로고    scopus 로고
    • Myosin 5b loss of function leads to defects in polarized signalling: implication for microvillus inclusion disease pathogenesis and treatment
    • Kravtsov D., Mashukova A., Forteza R., et al. Myosin 5b loss of function leads to defects in polarized signalling: implication for microvillus inclusion disease pathogenesis and treatment. Am J Physiol Gastrointest Liver Physiol 2014, 307:G992-G1001.
    • (2014) Am J Physiol Gastrointest Liver Physiol , vol.307 , pp. G992-G1001
    • Kravtsov, D.1    Mashukova, A.2    Forteza, R.3
  • 8
    • 84889575311 scopus 로고    scopus 로고
    • Microvillus inclusion disease: loss of myosin Vb disrupts intracellular traffic and cell polarity
    • Thoeni C.E., Vogel G.F., Tancevski I., et al. Microvillus inclusion disease: loss of myosin Vb disrupts intracellular traffic and cell polarity. Traffic 2013, 15:22-42.
    • (2013) Traffic , vol.15 , pp. 22-42
    • Thoeni, C.E.1    Vogel, G.F.2    Tancevski, I.3
  • 9
    • 84902992066 scopus 로고    scopus 로고
    • Myosin Vb uncoupling from RAB8A and RAB11A elicits microvillus inclusion disease
    • Knowles B.C., Roland J.T., Krishnan M., et al. Myosin Vb uncoupling from RAB8A and RAB11A elicits microvillus inclusion disease. J Clin Invest 2014, 124:2947-2962.
    • (2014) J Clin Invest , vol.124 , pp. 2947-2962
    • Knowles, B.C.1    Roland, J.T.2    Krishnan, M.3
  • 10
    • 84937917079 scopus 로고    scopus 로고
    • Myo5b knockout mice as a model of microvillus inclusion disease
    • Carton-Garcia F., Overeem A.W., Nieto R., et al. Myo5b knockout mice as a model of microvillus inclusion disease. Sci Rep 2015, 5:12312.
    • (2015) Sci Rep , vol.5 , pp. 12312
    • Carton-Garcia, F.1    Overeem, A.W.2    Nieto, R.3
  • 11
    • 84943370122 scopus 로고    scopus 로고
    • An inducible mouse model for microvillus inclusion disease reveals a role for myosin Vb in apical and basolateral trafficking
    • Schneeberger K., Vogel G.F., Teunissen H., et al. An inducible mouse model for microvillus inclusion disease reveals a role for myosin Vb in apical and basolateral trafficking. Proc Natl Acad Sci U S A 2015, 112:12408-12413.
    • (2015) Proc Natl Acad Sci U S A , vol.112 , pp. 12408-12413
    • Schneeberger, K.1    Vogel, G.F.2    Teunissen, H.3
  • 12
    • 84862517552 scopus 로고    scopus 로고
    • Phosphorylation of Rab11-FIP2 regulates polarity in MDCK cells
    • Lapierre L.A., Avant K.M., Caldwell C.M., et al. Phosphorylation of Rab11-FIP2 regulates polarity in MDCK cells. Mol Biol Cell 2012, 23:2302-2318.
    • (2012) Mol Biol Cell , vol.23 , pp. 2302-2318
    • Lapierre, L.A.1    Avant, K.M.2    Caldwell, C.M.3
  • 13
    • 34547810829 scopus 로고    scopus 로고
    • Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3
    • Roland J.T., Kenworthy A.K., Peranen J., et al. Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3. Mol Biol Cell 2007, 18:2828-2837.
    • (2007) Mol Biol Cell , vol.18 , pp. 2828-2837
    • Roland, J.T.1    Kenworthy, A.K.2    Peranen, J.3
  • 14
    • 84896892290 scopus 로고    scopus 로고
    • Myosin Vb and Rab11a regulate phosphorylation of ezrin in enterocytes
    • Dhekne H.S., Hsiao N.H., Roelofs P., et al. Myosin Vb and Rab11a regulate phosphorylation of ezrin in enterocytes. J Cell Sci 2014, 127:1007-1017.
    • (2014) J Cell Sci , vol.127 , pp. 1007-1017
    • Dhekne, H.S.1    Hsiao, N.H.2    Roelofs, P.3
  • 15
    • 2942622503 scopus 로고    scopus 로고
    • Ezrin is essential for epithelial organization and villus morphogenesis in the developing intestine
    • Saotome I., Curto M., McClatchey A.I. Ezrin is essential for epithelial organization and villus morphogenesis in the developing intestine. Dev Cell 2004, 6:855-864.
    • (2004) Dev Cell , vol.6 , pp. 855-864
    • Saotome, I.1    Curto, M.2    McClatchey, A.I.3
  • 16
    • 0036301282 scopus 로고    scopus 로고
    • CD10: a valuable tool for the light microscopic diagnosis of microvillous inclusion disease (familial microvillous atrophy)
    • Groisman G.M., Amar M., Livne E. CD10: a valuable tool for the light microscopic diagnosis of microvillous inclusion disease (familial microvillous atrophy). Am J Surg Pathol 2002, 26:902-907.
    • (2002) Am J Surg Pathol , vol.26 , pp. 902-907
    • Groisman, G.M.1    Amar, M.2    Livne, E.3
  • 17
    • 84928546261 scopus 로고    scopus 로고
    • Rab11a regulates syntaxin 3 localization and microvillus assembly in enterocytes
    • Knowles B.C., Weis V.G., Yu S., et al. Rab11a regulates syntaxin 3 localization and microvillus assembly in enterocytes. J Cell Sci 2015, 128:1617-1626.
    • (2015) J Cell Sci , vol.128 , pp. 1617-1626
    • Knowles, B.C.1    Weis, V.G.2    Yu, S.3
  • 18
    • 84979763374 scopus 로고    scopus 로고
    • Rab11a is required for apical protein localisation in the intestine
    • Sobajima T., Yoshimura S., Iwano T., et al. Rab11a is required for apical protein localisation in the intestine. Biol Open 2014, 4:86-94.
    • (2014) Biol Open , vol.4 , pp. 86-94
    • Sobajima, T.1    Yoshimura, S.2    Iwano, T.3
  • 19
    • 0015421358 scopus 로고
    • The mechanism of intestinal uptake and transcellular transport of IgG in the neonatal rat
    • Jones E.A., Waldmann T.A. The mechanism of intestinal uptake and transcellular transport of IgG in the neonatal rat. J Clin Invest 1972, 51:2916-2927.
    • (1972) J Clin Invest , vol.51 , pp. 2916-2927
    • Jones, E.A.1    Waldmann, T.A.2
  • 20
    • 0030880901 scopus 로고    scopus 로고
    • Expression of the neonatal Fc receptor, FcRn, on human intestinal epithelial cells
    • Israel E.J., Taylor S., Wu Z., et al. Expression of the neonatal Fc receptor, FcRn, on human intestinal epithelial cells. Immunology 1997, 92:69-74.
    • (1997) Immunology , vol.92 , pp. 69-74
    • Israel, E.J.1    Taylor, S.2    Wu, Z.3
  • 21
    • 0024529856 scopus 로고
    • An Fc receptor structurally related to MHC class I antigens
    • Simister N.E., Mostov K.E. An Fc receptor structurally related to MHC class I antigens. Nature 1989, 337:184-187.
    • (1989) Nature , vol.337 , pp. 184-187
    • Simister, N.E.1    Mostov, K.E.2
  • 22
    • 0028135495 scopus 로고
    • Paneth cell differentiation in the developing intestine of normal and transgenic mice
    • Bry L., Falk P., Huttner K., et al. Paneth cell differentiation in the developing intestine of normal and transgenic mice. Proc Natl Acad Sci U S A 1994, 91:10335-10339.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10335-10339
    • Bry, L.1    Falk, P.2    Huttner, K.3
  • 23
    • 0037317875 scopus 로고    scopus 로고
    • Distribution of the IgG Fc receptor, FcRn, in the human fetal intestine
    • Shah U., Dickinson B.L., Blumberg R.S., et al. Distribution of the IgG Fc receptor, FcRn, in the human fetal intestine. Pediatr Res 2003, 53:295-301.
    • (2003) Pediatr Res , vol.53 , pp. 295-301
    • Shah, U.1    Dickinson, B.L.2    Blumberg, R.S.3
  • 24
    • 0015877138 scopus 로고
    • Intestinal transport of antibodies in the newborn rat
    • Rodewald R. Intestinal transport of antibodies in the newborn rat. J Cell Biol 1973, 58:189-211.
    • (1973) J Cell Biol , vol.58 , pp. 189-211
    • Rodewald, R.1
  • 25
    • 52949110519 scopus 로고    scopus 로고
    • FcRn-mediated antibody transport across epithelial cells revealed by electron tomography
    • He W., Ladinsky M.S., Huey-Tubman K.E., et al. FcRn-mediated antibody transport across epithelial cells revealed by electron tomography. Nature 2008, 455:542-546.
    • (2008) Nature , vol.455 , pp. 542-546
    • He, W.1    Ladinsky, M.S.2    Huey-Tubman, K.E.3
  • 26
    • 70649111219 scopus 로고    scopus 로고
    • Effects of endocytosis inhibitors on internalization of human IgG by Caco-2 human intestinal epithelial cells
    • Sato K., Nagai J., Mitsui N., et al. Effects of endocytosis inhibitors on internalization of human IgG by Caco-2 human intestinal epithelial cells. Life Sci 2009, 85:800-807.
    • (2009) Life Sci , vol.85 , pp. 800-807
    • Sato, K.1    Nagai, J.2    Mitsui, N.3
  • 27
    • 84975193726 scopus 로고    scopus 로고
    • Cargo-selective apical exocytosis in epithelial cells is conducted by Myo5B, Slp4a, Vamp7, and Syntaxin 3
    • Vogel G.F., Klee K.M., Janecke A.R., et al. Cargo-selective apical exocytosis in epithelial cells is conducted by Myo5B, Slp4a, Vamp7, and Syntaxin 3. J Cell Biol 2015, 211:587-604.
    • (2015) J Cell Biol , vol.211 , pp. 587-604
    • Vogel, G.F.1    Klee, K.M.2    Janecke, A.R.3
  • 28
    • 0021815019 scopus 로고
    • Congenital microvillous atrophy: specific diagnostic features
    • Phillips A.D., Jenkins P., Raafat F., et al. Congenital microvillous atrophy: specific diagnostic features. Arch Dis Child 1985, 60:135-140.
    • (1985) Arch Dis Child , vol.60 , pp. 135-140
    • Phillips, A.D.1    Jenkins, P.2    Raafat, F.3
  • 29
    • 0023925133 scopus 로고
    • Single-villus analysis of disaccharidase expression by different regions of the mouse intestine
    • James P.S., Smith M.W., Tivey D.R. Single-villus analysis of disaccharidase expression by different regions of the mouse intestine. J Physiol 1988, 401:533-545.
    • (1988) J Physiol , vol.401 , pp. 533-545
    • James, P.S.1    Smith, M.W.2    Tivey, D.R.3
  • 30
    • 0014056194 scopus 로고
    • Structural and functional changes following small intestinal resection in the rat
    • Dowling R.H., Booth C.C. Structural and functional changes following small intestinal resection in the rat. Clin Sci 1967, 32:139-149.
    • (1967) Clin Sci , vol.32 , pp. 139-149
    • Dowling, R.H.1    Booth, C.C.2
  • 31
    • 32144445923 scopus 로고    scopus 로고
    • Mechanisms of enteral nutrient-enhanced intestinal adaptation
    • Tappenden K.A. Mechanisms of enteral nutrient-enhanced intestinal adaptation. Gastroenterology 2006, 130:S93-S99.
    • (2006) Gastroenterology , vol.130 , pp. S93-S99
    • Tappenden, K.A.1
  • 32
    • 34247532276 scopus 로고    scopus 로고
    • Impact of caloric intake on parenteral nutrition-associated intestinal morphology and mucosal barrier function
    • Sun X., Spencer A.U., Yang H., et al. Impact of caloric intake on parenteral nutrition-associated intestinal morphology and mucosal barrier function. JPEN J Parenter Enteral Nutr 2006, 30:474-479.
    • (2006) JPEN J Parenter Enteral Nutr , vol.30 , pp. 474-479
    • Sun, X.1    Spencer, A.U.2    Yang, H.3
  • 33
    • 0033664449 scopus 로고    scopus 로고
    • Quantitative study of changes in intestinal morphology and mucus gel on total parenteral nutrition in rats
    • Sakamoto K., Hirose H., Onizuka A., et al. Quantitative study of changes in intestinal morphology and mucus gel on total parenteral nutrition in rats. J Surg Res 2000, 94:99-106.
    • (2000) J Surg Res , vol.94 , pp. 99-106
    • Sakamoto, K.1    Hirose, H.2    Onizuka, A.3
  • 34
    • 0028826638 scopus 로고
    • Parenteral nutrition is associated with intestinal morphologic and functional changes in humans
    • Buchman A.L., Moukarzel A.A., Bhuta S., et al. Parenteral nutrition is associated with intestinal morphologic and functional changes in humans. JPEN J Parenter Enteral Nutr 1995, 19:453-460.
    • (1995) JPEN J Parenter Enteral Nutr , vol.19 , pp. 453-460
    • Buchman, A.L.1    Moukarzel, A.A.2    Bhuta, S.3
  • 35
    • 59649128714 scopus 로고    scopus 로고
    • Dissociation of E-cadherin and beta-catenin in a mouse model of total parenteral nutrition: a mechanism for the loss of epithelial cell proliferation and villus atrophy
    • Feng Y., Sun X., Yang H., et al. Dissociation of E-cadherin and beta-catenin in a mouse model of total parenteral nutrition: a mechanism for the loss of epithelial cell proliferation and villus atrophy. J Physiol 2009, 587:641-654.
    • (2009) J Physiol , vol.587 , pp. 641-654
    • Feng, Y.1    Sun, X.2    Yang, H.3
  • 36
    • 84903174800 scopus 로고    scopus 로고
    • MYO5B and bile salt export pump contribute to cholestatic liver disorder in microvillous inclusion disease
    • Girard M., Lacaille F., Verkarre V., et al. MYO5B and bile salt export pump contribute to cholestatic liver disorder in microvillous inclusion disease. Hepatology 2014, 60:301-310.
    • (2014) Hepatology , vol.60 , pp. 301-310
    • Girard, M.1    Lacaille, F.2    Verkarre, V.3
  • 37
    • 27244439821 scopus 로고    scopus 로고
    • Rab11a and myosin Vb are required for bile canalicular formation in WIF-B9 cells
    • Wakabayashi Y., Dutt P., Lippincott-Schwartz J., et al. Rab11a and myosin Vb are required for bile canalicular formation in WIF-B9 cells. Proc Natl Acad Sci U S A 2005, 102:15087-15092.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15087-15092
    • Wakabayashi, Y.1    Dutt, P.2    Lippincott-Schwartz, J.3


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