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Volumn 14, Issue 6, 2004, Pages 312-319

LKB1 tumor suppressor protein: PARtaker in cell polarity

Author keywords

[No Author keywords available]

Indexed keywords

HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; PAR1 PROTEIN; PROTEIN; PROTEIN KINASE LKB1; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 2942729619     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2004.04.001     Document Type: Review
Times cited : (116)

References (92)
  • 1
    • 0000043603 scopus 로고
    • On a very remarkable case of familial polyposis of the mucous membrane of the intestinal tract and nasopharynx accompanied by peculiar pigmentation of the skin and mucous membranes
    • Peutz J.L. On a very remarkable case of familial polyposis of the mucous membrane of the intestinal tract and nasopharynx accompanied by peculiar pigmentation of the skin and mucous membranes. Ned. Tijdschr. Geneeskd. 10:1921;134-146
    • (1921) Ned. Tijdschr. Geneeskd. , vol.10 , pp. 134-146
    • Peutz, J.L.1
  • 2
    • 0000152019 scopus 로고
    • Generalised intestinal polyposis and melanin spots of oral mucosa, lips and digits: A syndrome of diagnostic significance
    • Jeghers H., et al. Generalised intestinal polyposis and melanin spots of oral mucosa, lips and digits: a syndrome of diagnostic significance. N. Engl. J. Med. 241:1949;992-1005
    • (1949) N. Engl. J. Med. , vol.241 , pp. 992-1005
    • Jeghers, H.1
  • 3
    • 0034464147 scopus 로고    scopus 로고
    • Very high risk of cancer in familial Peutz-Jeghers syndrome
    • Giardiello F.M., et al. Very high risk of cancer in familial Peutz-Jeghers syndrome. Gastroenterology. 119:2000;1447-1453
    • (2000) Gastroenterology , vol.119 , pp. 1447-1453
    • Giardiello, F.M.1
  • 4
    • 0032495530 scopus 로고    scopus 로고
    • A serine/threonine kinase gene defective in Peutz-Jeghers syndrome
    • Hemminki A., et al. A serine/threonine kinase gene defective in Peutz-Jeghers syndrome. Nature. 391:1998;184-187
    • (1998) Nature , vol.391 , pp. 184-187
    • Hemminki, A.1
  • 5
    • 0031974516 scopus 로고    scopus 로고
    • Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase
    • Jenne D.E., et al. Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase. Nat. Genet. 18:1998;38-43
    • (1998) Nat. Genet. , vol.18 , pp. 38-43
    • Jenne, D.E.1
  • 6
    • 0033522144 scopus 로고    scopus 로고
    • Somatic mutations of the Peutz-Jeghers gene in malignant melanoma
    • Guldberg P., et al. Somatic mutations of the Peutz-Jeghers gene in malignant melanoma. Oncogene. 18:1999;1777-1780
    • (1999) Oncogene , vol.18 , pp. 1777-1780
    • Guldberg, P.1
  • 7
    • 0032984141 scopus 로고    scopus 로고
    • Germline and somatic mutations of the STK11/LKB1 Peutz Jeghers gene in pancreatic and biliary cancers
    • Su G.H., et al. Germline and somatic mutations of the STK11/LKB1 Peutz Jeghers gene in pancreatic and biliary cancers. Am. J. Pathol. 154:1999;1835-1840
    • (1999) Am. J. Pathol. , vol.154 , pp. 1835-1840
    • Su, G.H.1
  • 8
    • 0036645286 scopus 로고    scopus 로고
    • Inactivation of LKB1/STK11 is a common event in adenocarcinomas of the lung
    • Sanchez-Cespedes M., et al. Inactivation of LKB1/STK11 is a common event in adenocarcinomas of the lung. Cancer Res. 62:2002;3659-3662
    • (2002) Cancer Res. , vol.62 , pp. 3659-3662
    • Sanchez-Cespedes, M.1
  • 9
    • 0036172159 scopus 로고    scopus 로고
    • Establishing cell polarity in development
    • Wodarz A. Establishing cell polarity in development. Nat. Cell Biol. 4:2002;E39-E44
    • (2002) Nat. Cell Biol. , vol.4 , pp. 39-E44
    • Wodarz, A.1
  • 10
    • 0034618663 scopus 로고    scopus 로고
    • Tumor suppressors: Linking cell polarity and growth control
    • Wodarz A. Tumor suppressors: linking cell polarity and growth control. Curr. Biol. 10:2000;R624-R626
    • (2000) Curr. Biol. , vol.10 , pp. 624-R626
    • Wodarz, A.1
  • 11
    • 0036595629 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in tumour progression
    • Thiery J.P. Epithelial-mesenchymal transitions in tumour progression. Nat. Rev. Cancer. 2:2002;442-454
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 442-454
    • Thiery, J.P.1
  • 12
    • 1542777034 scopus 로고    scopus 로고
    • Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD
    • Baas A.F., et al. Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD. Cell. 116:2004;457-466
    • (2004) Cell , vol.116 , pp. 457-466
    • Baas, A.F.1
  • 13
    • 0035903028 scopus 로고    scopus 로고
    • Vascular abnormalities and deregulation of VEGF in Lkb1-deficient mice
    • Ylikorkala A., et al. Vascular abnormalities and deregulation of VEGF in Lkb1-deficient mice. Science. 293:2001;1323-1326
    • (2001) Science , vol.293 , pp. 1323-1326
    • Ylikorkala, A.1
  • 14
    • 0037068461 scopus 로고    scopus 로고
    • Loss of the Lkb1 tumour suppressor provokes intestinal polyposis but resistance to transformation
    • Bardeesy N., et al. Loss of the Lkb1 tumour suppressor provokes intestinal polyposis but resistance to transformation. Nature. 419:2002;162-167
    • (2002) Nature , vol.419 , pp. 162-167
    • Bardeesy, N.1
  • 15
    • 0037173013 scopus 로고    scopus 로고
    • Role of Lkb1, the causative gene of Peutz-Jeghers syndrome, in embryogenesis and polyposis
    • Jishage K., et al. Role of Lkb1, the causative gene of Peutz-Jeghers syndrome, in embryogenesis and polyposis. Proc. Natl. Acad. Sci. U. S. A. 99:2002;8903-8908
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 8903-8908
    • Jishage, K.1
  • 16
    • 0037089467 scopus 로고    scopus 로고
    • Gastrointestinal hamartomatous polyposis in Lkb1 heterozygous knockout mice
    • Miyoshi H., et al. Gastrointestinal hamartomatous polyposis in Lkb1 heterozygous knockout mice. Cancer Res. 62:2002;2261-2266
    • (2002) Cancer Res. , vol.62 , pp. 2261-2266
    • Miyoshi, H.1
  • 17
    • 0037125996 scopus 로고    scopus 로고
    • Induction of cyclooxygenase-2 in a mouse model of Peutz-Jeghers polyposis
    • Rossi D.J., et al. Induction of cyclooxygenase-2 in a mouse model of Peutz-Jeghers polyposis. Proc. Natl. Acad. Sci. U. S. A. 99:2002;12327-12332
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12327-12332
    • Rossi, D.J.1
  • 18
    • 0037102428 scopus 로고    scopus 로고
    • Hepatocellular carcinoma caused by loss of heterozygosity in lkb1 gene knockout mice
    • Nakau M., et al. Hepatocellular carcinoma caused by loss of heterozygosity in lkb1 gene knockout mice. Cancer Res. 62:2002;4549-4553
    • (2002) Cancer Res. , vol.62 , pp. 4549-4553
    • Nakau, M.1
  • 19
    • 0034090975 scopus 로고    scopus 로고
    • The C. elegans par-40 gene encodes a putative serine-threonine kinase required for establishing embryonic asymmetry
    • Watts J.L., et al. The C. elegans par-40 gene encodes a putative serine-threonine kinase required for establishing embryonic asymmetry. Development. 127:2000;1467-1475
    • (2000) Development , vol.127 , pp. 1467-1475
    • Watts, J.L.1
  • 20
    • 0024284814 scopus 로고
    • Identification of genes required for cytoplasmic localization in early C. elegans embryos
    • Kemphues K.J., et al. Identification of genes required for cytoplasmic localization in early C. elegans embryos. Cell. 52:1988;311-320
    • (1988) Cell , vol.52 , pp. 311-320
    • Kemphues, K.J.1
  • 21
    • 0037461735 scopus 로고    scopus 로고
    • A role for Drosophila LKB1 in anterior-posterior axis formation and epithelial polarity
    • Martin S.G., St Johnston D. A role for Drosophila LKB1 in anterior-posterior axis formation and epithelial polarity. Nature. 421:2003;379-384
    • (2003) Nature , vol.421 , pp. 379-384
    • Martin, S.G.1    St Johnston, D.2
  • 22
    • 0033529838 scopus 로고    scopus 로고
    • Growth suppression by Lkb1 is mediated by a G(1) cell cycle arrest
    • Tiainen M., et al. Growth suppression by Lkb1 is mediated by a G(1) cell cycle arrest. Proc. Natl. Acad. Sci. U. S. A. 96:1999;9248-9251
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9248-9251
    • Tiainen, M.1
  • 23
    • 0034964446 scopus 로고    scopus 로고
    • The Peutz-Jegher gene product LKB1 is a mediator of p53-dependent cell death
    • Karuman P., et al. The Peutz-Jegher gene product LKB1 is a mediator of p53-dependent cell death. Mol. Cell. 7:2001;1307-1319
    • (2001) Mol. Cell , vol.7 , pp. 1307-1319
    • Karuman, P.1
  • 24
    • 0042090214 scopus 로고    scopus 로고
    • Regulation of the Wnt signalling component PAR1A by the Peutz-Jeghers syndrome kinase LKB1
    • Spicer J., et al. Regulation of the Wnt signalling component PAR1A by the Peutz-Jeghers syndrome kinase LKB1. Oncogene. 22:2003;4752-4756
    • (2003) Oncogene , vol.22 , pp. 4752-4756
    • Spicer, J.1
  • 25
    • 0141616620 scopus 로고    scopus 로고
    • LKB1 (XEEK1) regulates Wnt signalling in vertebrate development
    • Ossipova O., et al. LKB1 (XEEK1) regulates Wnt signalling in vertebrate development. Nat. Cell Biol. 5:2003;889-894
    • (2003) Nat. Cell Biol. , vol.5 , pp. 889-894
    • Ossipova, O.1
  • 26
    • 0035660222 scopus 로고    scopus 로고
    • LIP1, a cytoplasmic protein functionally linked to the Peutz-Jeghers syndrome kinase LKB1
    • Smith D.P., et al. LIP1, a cytoplasmic protein functionally linked to the Peutz-Jeghers syndrome kinase LKB1. Hum. Mol. Genet. 10:2001;2869-2877
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2869-2877
    • Smith, D.P.1
  • 27
    • 0345107247 scopus 로고    scopus 로고
    • Complexes between the LKB1 tumor suppressor, STRADalpha/beta and MO25alpha/beta are upstream kinases in the AMP-activated protein kinase cascade
    • Hawley S.A., et al. Complexes between the LKB1 tumor suppressor, STRADalpha/beta and MO25alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J. Biol. 2:2003;28
    • (2003) J. Biol. , vol.2 , pp. 28
    • Hawley, S.A.1
  • 28
    • 10744230065 scopus 로고    scopus 로고
    • LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
    • Woods A., et al. LKB1 is the upstream kinase in the AMP-activated protein kinase cascade. Curr. Biol. 13:2003;2004-2008
    • (2003) Curr. Biol. , vol.13 , pp. 2004-2008
    • Woods, A.1
  • 29
    • 1542618348 scopus 로고    scopus 로고
    • The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress
    • Shaw R.J., et al. The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress. Proc. Natl. Acad. Sci. U. S. A. 101:2004;3329-3335
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 3329-3335
    • Shaw, R.J.1
  • 30
    • 0037096833 scopus 로고    scopus 로고
    • Growth arrest by the LKB1 tumor suppressor: Induction of p21(WAF1/CIP1)
    • Tiainen M., et al. Growth arrest by the LKB1 tumor suppressor: induction of p21(WAF1/CIP1). Hum. Mol. Genet. 11:2002;1497-1504
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1497-1504
    • Tiainen, M.1
  • 31
    • 0035980097 scopus 로고    scopus 로고
    • LKB1 associates with Brg1 and is necessary for Brg1-induced growth arrest
    • Marignani P.A., et al. LKB1 associates with Brg1 and is necessary for Brg1-induced growth arrest. J. Biol. Chem. 276:2001;32415-32418
    • (2001) J. Biol. Chem. , vol.276 , pp. 32415-32418
    • Marignani, P.A.1
  • 32
    • 0037444766 scopus 로고    scopus 로고
    • Heat shock protein 90 and Cdc37 interact with LKB1 and regulate its stability
    • Boudeau J., et al. Heat shock protein 90 and Cdc37 interact with LKB1 and regulate its stability. Biochem. J. 370:2003;849-857
    • (2003) Biochem. J. , vol.370 , pp. 849-857
    • Boudeau, J.1
  • 33
    • 0346057795 scopus 로고    scopus 로고
    • Stability of the Peutz-Jeghers syndrome kinase LKB1 requires its binding to the molecular chaperones Hsp90/Cdc37
    • Nony P., et al. Stability of the Peutz-Jeghers syndrome kinase LKB1 requires its binding to the molecular chaperones Hsp90/Cdc37. Oncogene. 22:2003;9165-9175
    • (2003) Oncogene , vol.22 , pp. 9165-9175
    • Nony, P.1
  • 34
    • 0037593654 scopus 로고    scopus 로고
    • Interaction of activator of G-protein signaling 3 (AGS3) with LKB1, a serine/threonine kinase involved in cell polarity and cell cycle progression: Phosphorylation of the G-protein regulatory (GPR) motif as a regulatory mechanism for the interaction of GPR motifs with Gi alpha
    • Blumer J.B., et al. Interaction of activator of G-protein signaling 3 (AGS3) with LKB1, a serine/threonine kinase involved in cell polarity and cell cycle progression: phosphorylation of the G-protein regulatory (GPR) motif as a regulatory mechanism for the interaction of GPR motifs with Gi alpha. J. Biol. Chem. 278:2003;23217-23220
    • (2003) J. Biol. Chem. , vol.278 , pp. 23217-23220
    • Blumer, J.B.1
  • 35
    • 0038614742 scopus 로고    scopus 로고
    • Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD
    • Baas A.F., et al. Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD. EMBO J. 22:2003;3062-3072
    • (2003) EMBO J. , vol.22 , pp. 3062-3072
    • Baas, A.F.1
  • 36
    • 0141753981 scopus 로고    scopus 로고
    • MO25α/β interact with STRADα/β enhancing their ability to bind, activate and localise LKB1 in the cytoplasm
    • Boudeau J., et al. MO25α/β interact with STRADα/β enhancing their ability to bind, activate and localise LKB1 in the cytoplasm. EMBO J. 22:2003;3062-3072
    • (2003) EMBO J. , vol.22 , pp. 3062-3072
    • Boudeau, J.1
  • 37
    • 0037163015 scopus 로고    scopus 로고
    • ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated activation of JNK1 and protection against apoptosis
    • Sanna M.G., et al. ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated activation of JNK1 and protection against apoptosis. J. Biol. Chem. 277:2002;30454-30462
    • (2002) J. Biol. Chem. , vol.277 , pp. 30454-30462
    • Sanna, M.G.1
  • 38
    • 0038305886 scopus 로고    scopus 로고
    • Identification and characterization of a novel Ste-20/GCK-related kinase, PAP kinase (PAPK)
    • Nishigaki K., et al. Identification and characterization of a novel Ste-20/GCK-related kinase, PAP kinase (PAPK). J. Biol. Chem. 278:2003;13520-13530
    • (2003) J. Biol. Chem. , vol.278 , pp. 13520-13530
    • Nishigaki, K.1
  • 39
    • 0035341895 scopus 로고    scopus 로고
    • The Ste20 group kinases as regulators of MAP kinase cascades
    • Dan I., et al. The Ste20 group kinases as regulators of MAP kinase cascades. Trends Cell Biol. 11:2001;220-230
    • (2001) Trends Cell Biol. , vol.11 , pp. 220-230
    • Dan, I.1
  • 40
    • 0030002157 scopus 로고    scopus 로고
    • Identification and characterization of the Drosophila Mo25 gene, which is conserved among Drosophila, mouse and yeast
    • Nozaki M., et al. Identification and characterization of the Drosophila Mo25 gene, which is conserved among Drosophila, mouse and yeast. DNA Cell Biol. 15:1996;505-509
    • (1996) DNA Cell Biol. , vol.15 , pp. 505-509
    • Nozaki, M.1
  • 41
    • 1842581909 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network
    • Brajenovic M., et al. Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network. J. Biol. Chem. 279:2003;12804-12811
    • (2003) J. Biol. Chem. , vol.279 , pp. 12804-12811
    • Brajenovic, M.1
  • 42
    • 0038199737 scopus 로고    scopus 로고
    • Management of cellular energy by the AMP-activated protein kinase system
    • Hardie D.G., et al. Management of cellular energy by the AMP-activated protein kinase system. FEBS Lett. 546:2003;113-120
    • (2003) FEBS Lett. , vol.546 , pp. 113-120
    • Hardie, D.G.1
  • 43
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the AMP-activated protein kinase kinase from rat liver, and identification of threonine-172 as the major site at which it phosphorylates and activates AMP-activated protein kinase
    • Hawley S.A., et al. Characterization of the AMP-activated protein kinase kinase from rat liver, and identification of threonine-172 as the major site at which it phosphorylates and activates AMP-activated protein kinase. J. Biol. Chem. 271:1996;27879-27887
    • (1996) J. Biol. Chem. , vol.271 , pp. 27879-27887
    • Hawley, S.A.1
  • 44
    • 0033565773 scopus 로고    scopus 로고
    • Kinase phosphorylation: Keeping it all in the family
    • Peterson R.T., Schreiber S.L. Kinase phosphorylation: keeping it all in the family. Curr. Biol. 9:1999;R521-R524
    • (1999) Curr. Biol. , vol.9 , pp. 521-R524
    • Peterson, R.T.1    Schreiber, S.L.2
  • 45
    • 12144287284 scopus 로고    scopus 로고
    • LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1
    • Lizcano J.M., et al. LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1. EMBO J. 23:2004;833-843
    • (2004) EMBO J. , vol.23 , pp. 833-843
    • Lizcano, J.M.1
  • 46
    • 0029024475 scopus 로고
    • Par-1, a gene required for establishing polarity in C. elegans embryos, encodes a putative Ser/Thr kinase that is asymmetrically distributed
    • Guo S., Kemphues K.J. Par-1, a gene required for establishing polarity in C. elegans embryos, encodes a putative Ser/Thr kinase that is asymmetrically distributed. Cell. 81:1995;611-620
    • (1995) Cell , vol.81 , pp. 611-620
    • Guo, S.1    Kemphues, K.J.2
  • 47
    • 0034640112 scopus 로고    scopus 로고
    • The Drosophila homolog of C. elegans PAR-1 organizes the oocyte cytoskeleton and directs oskar mRNA localization to the posterior pole
    • Shulman J.M., et al. The Drosophila homolog of C. elegans PAR-1 organizes the oocyte cytoskeleton and directs oskar mRNA localization to the posterior pole. Cell. 101:2000;377-388
    • (2000) Cell , vol.101 , pp. 377-388
    • Shulman, J.M.1
  • 48
    • 0033775722 scopus 로고    scopus 로고
    • A Drosophila melanogaster homologue of Caenorhabditis elegans par-1 acts at an early step in embryonic-axis formation
    • Tomancak P., et al. A Drosophila melanogaster homologue of Caenorhabditis elegans par-1 acts at an early step in embryonic-axis formation. Nat. Cell Biol. 2:2000;458-460
    • (2000) Nat. Cell Biol. , vol.2 , pp. 458-460
    • Tomancak, P.1
  • 49
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes G., et al. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell. 89:1997;297-308
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1
  • 50
    • 0036854327 scopus 로고    scopus 로고
    • Protein kinase MARK/PAR-1 is required for neurite outgrowth and establishment of neuronal polarity
    • Biernat J., et al. Protein kinase MARK/PAR-1 is required for neurite outgrowth and establishment of neuronal polarity. Mol. Biol. Cell. 13:2002;4013-4028
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4013-4028
    • Biernat, J.1
  • 51
    • 0036147620 scopus 로고    scopus 로고
    • The Caenorhabditis elegans par-5 gene encodes a 14-3-3 protein required for cellular asymmetry in the early embryo
    • Morton D.G., et al. The Caenorhabditis elegans par-5 gene encodes a 14-3-3 protein required for cellular asymmetry in the early embryo. Dev. Biol. 241:2002;47-58
    • (2002) Dev. Biol. , vol.241 , pp. 47-58
    • Morton, D.G.1
  • 52
    • 0029850113 scopus 로고    scopus 로고
    • Par-6, a gene involved in the establishment of asymmetry in early C. elegans embryos, mediates the asymmetric localization of PAR-3
    • Watts J.L., et al. Par-6, a gene involved in the establishment of asymmetry in early C. elegans embryos, mediates the asymmetric localization of PAR-3. Development. 122:1996;3133-3140
    • (1996) Development , vol.122 , pp. 3133-3140
    • Watts, J.L.1
  • 53
    • 0032426346 scopus 로고    scopus 로고
    • Early patterning of the C. elegans embryo
    • Rose L.S., Kemphues K.J. Early patterning of the C. elegans embryo. Annu. Rev. Genet. 32:1998;521-545
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 521-545
    • Rose, L.S.1    Kemphues, K.J.2
  • 54
    • 0346155807 scopus 로고    scopus 로고
    • Cell polarity and the cytoskeleton in the Caenorhabditis elegans zygote
    • Schneider S.Q., Bowerman B. Cell polarity and the cytoskeleton in the Caenorhabditis elegans zygote. Annu. Rev. Genet. 37:2003;221-249
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 221-249
    • Schneider, S.Q.1    Bowerman, B.2
  • 55
    • 10344236460 scopus 로고    scopus 로고
    • PAR-2 is asymmetrically distributed and promotes association of P granules and PAR-1 with the cortex in C. elegans embryos
    • Boyd L., et al. PAR-2 is asymmetrically distributed and promotes association of P granules and PAR-1 with the cortex in C. elegans embryos. Development. 122:1996;3075-3084
    • (1996) Development , vol.122 , pp. 3075-3084
    • Boyd, L.1
  • 56
    • 0028843736 scopus 로고
    • Asymmetrically distributed PAR-3 protein contributes to cell polarity and spindle alignment in early C. elegans embryos
    • Etemad-Moghadam B., et al. Asymmetrically distributed PAR-3 protein contributes to cell polarity and spindle alignment in early C. elegans embryos. Cell. 83:1995;743-752
    • (1995) Cell , vol.83 , pp. 743-752
    • Etemad-Moghadam, B.1
  • 57
    • 0031674842 scopus 로고    scopus 로고
    • Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans
    • Tabuse Y., et al. Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans. Development. 125:1998;3607-3614
    • (1998) Development , vol.125 , pp. 3607-3614
    • Tabuse, Y.1
  • 58
    • 0037032795 scopus 로고    scopus 로고
    • Anterior-posterior polarity in C. elegans and Drosophila - PARallels and differences
    • Pellettieri J., Seydoux G. Anterior-posterior polarity in C. elegans and Drosophila - PARallels and differences. Science. 298:2002;1946-1950
    • (2002) Science , vol.298 , pp. 1946-1950
    • Pellettieri, J.1    Seydoux, G.2
  • 59
    • 0032949091 scopus 로고    scopus 로고
    • PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos
    • Hung T.J., Kemphues K.J. PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos. Development. 126:1999;127-135
    • (1999) Development , vol.126 , pp. 127-135
    • Hung, T.J.1    Kemphues, K.J.2
  • 60
    • 0032585579 scopus 로고    scopus 로고
    • Control of spindle orientation in Drosophila by the Par-3-related PDZ-domain protein Bazooka
    • Kuchinke U., et al. Control of spindle orientation in Drosophila by the Par-3-related PDZ-domain protein Bazooka. Curr. Biol. 8:1998;1357-1365
    • (1998) Curr. Biol. , vol.8 , pp. 1357-1365
    • Kuchinke, U.1
  • 61
    • 0034683578 scopus 로고    scopus 로고
    • Drosophila atypical protein kinase C associates with Bazooka and controls polarity of epithelia and neuroblasts
    • Wodarz A., et al. Drosophila atypical protein kinase C associates with Bazooka and controls polarity of epithelia and neuroblasts. J. Cell Biol. 150:2000;1361-1374
    • (2000) J. Cell Biol. , vol.150 , pp. 1361-1374
    • Wodarz, A.1
  • 62
    • 0035141027 scopus 로고    scopus 로고
    • DmPAR-6 directs epithelial polarity and asymmetric cell division of neuroblasts in Drosophila
    • Petronczki M., Knoblich J.A. DmPAR-6 directs epithelial polarity and asymmetric cell division of neuroblasts in Drosophila. Nat. Cell Biol. 3:2001;43-49
    • (2001) Nat. Cell Biol. , vol.3 , pp. 43-49
    • Petronczki, M.1    Knoblich, J.A.2
  • 63
    • 0035811044 scopus 로고    scopus 로고
    • Bazooka and PAR-6 are required with PAR-1 for the maintenance of oocyte fate in Drosophila
    • Huyhn J.R., et al. Bazooka and PAR-6 are required with PAR-1 for the maintenance of oocyte fate in Drosophila. Curr. Biol. 11:2001;901-906
    • (2001) Curr. Biol. , vol.11 , pp. 901-906
    • Huyhn, J.R.1
  • 64
    • 0036847993 scopus 로고    scopus 로고
    • Drosophila 14-3-3/PAR-5 is an essential mediator of PAR-1 function in axis formation
    • Benton R., et al. Drosophila 14-3-3/PAR-5 is an essential mediator of PAR-1 function in axis formation. Dev. Cell. 3:2002;659-671
    • (2002) Dev. Cell , vol.3 , pp. 659-671
    • Benton, R.1
  • 65
    • 0035479930 scopus 로고    scopus 로고
    • Intercellular junctions and cellular polarity: The PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity
    • Ohno S. Intercellular junctions and cellular polarity: the PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity. Curr. Opin. Cell Biol. 13:2001;641-648
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 641-648
    • Ohno, S.1
  • 66
    • 0041827252 scopus 로고    scopus 로고
    • The role of PAR-1 in regulating the polarised microtubule cytoskeleton in the Drosophila follicular epithelium
    • Doerflinger H., et al. The role of PAR-1 in regulating the polarised microtubule cytoskeleton in the Drosophila follicular epithelium. Development. 130:2003;3965-3975
    • (2003) Development , vol.130 , pp. 3965-3975
    • Doerflinger, H.1
  • 67
    • 0347596668 scopus 로고    scopus 로고
    • Drosophila PAR-1 and 14-3-3 inhibit Bazooka/PAR-3 to establish complementary cortical domains in polarized cells
    • Benton R., St Johnston D.R. Drosophila PAR-1 and 14-3-3 inhibit Bazooka/PAR-3 to establish complementary cortical domains in polarized cells. Cell. 115:2003;691-704
    • (2003) Cell , vol.115 , pp. 691-704
    • Benton, R.1    St Johnston, D.R.2
  • 68
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin D.G., Nelson W.J. Origins of cell polarity. Cell. 84:1996;335-344
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 69
    • 0032956497 scopus 로고    scopus 로고
    • New perspectives on mechanisms involved in generating epithelial cell polarity
    • Yeaman C., et al. New perspectives on mechanisms involved in generating epithelial cell polarity. Physiol. Rev. 79:1999;73-98
    • (1999) Physiol. Rev. , vol.79 , pp. 73-98
    • Yeaman, C.1
  • 70
  • 71
    • 0026877444 scopus 로고
    • Classical cadherins
    • Kemler R. Classical cadherins. Semin. Cell Biol. 3:1992;149-155
    • (1992) Semin. Cell Biol. , vol.3 , pp. 149-155
    • Kemler, R.1
  • 72
    • 0034515183 scopus 로고    scopus 로고
    • Assembly of tight junctions during early vertebrate development
    • Fleming T.P., et al. Assembly of tight junctions during early vertebrate development. Semin. Cell Dev. Biol. 11:2000;291-299
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 291-299
    • Fleming, T.P.1
  • 73
    • 0034722381 scopus 로고    scopus 로고
    • Tight junction, a platform for trafficking and signaling protein complexes
    • Zahraoui A., et al. Tight junction, a platform for trafficking and signaling protein complexes. J. Cell Biol. 151:2000;F31-F36
    • (2000) J. Cell Biol. , vol.151 , pp. 31-F36
    • Zahraoui, A.1
  • 74
    • 0021067619 scopus 로고
    • Enterocyte-like differentiation and polarization of the human colon carcinoma cell line Caco-2 in culture
    • Pinto M., et al. Enterocyte-like differentiation and polarization of the human colon carcinoma cell line Caco-2 in culture. Biol. Cell. 47:1983;323-330
    • (1983) Biol. Cell. , vol.47 , pp. 323-330
    • Pinto, M.1
  • 75
    • 0018819280 scopus 로고
    • Structural and functional membrane polarity in cultured monolayers of MDCK cells
    • Cereijido M., et al. Structural and functional membrane polarity in cultured monolayers of MDCK cells. J. Membr. Biol. 52:1980;147-159
    • (1980) J. Membr. Biol. , vol.52 , pp. 147-159
    • Cereijido, M.1
  • 76
    • 0032487494 scopus 로고    scopus 로고
    • An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
    • Izumi Y. An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. J. Cell Biol. 143:1998;95-106
    • (1998) J. Cell Biol. , vol.143 , pp. 95-106
    • Izumi, Y.1
  • 77
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • Joberty G., et al. The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat. Cell Biol. 2:2000;531-539
    • (2000) Nat. Cell Biol. , vol.2 , pp. 531-539
    • Joberty, G.1
  • 78
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • Suzuki A., et al. Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J. Cell Biol. 152:2001;1183-1196
    • (2001) J. Cell Biol. , vol.152 , pp. 1183-1196
    • Suzuki, A.1
  • 79
    • 0034874862 scopus 로고    scopus 로고
    • PAR-6 regulates aPKC activity in a novel way and mediates cell-cell contact-induced formation of the epithelial junctional complex
    • Yamanaka T., et al. PAR-6 regulates aPKC activity in a novel way and mediates cell-cell contact-induced formation of the epithelial junctional complex. Genes Cells. 6:2001;721-731
    • (2001) Genes Cells , vol.6 , pp. 721-731
    • Yamanaka, T.1
  • 80
    • 0037022122 scopus 로고    scopus 로고
    • Assembly of epithelial tight junctions is negatively regulated by Par6
    • Gao L., et al. Assembly of epithelial tight junctions is negatively regulated by Par6. Curr. Biol. 12:2002;221-225
    • (2002) Curr. Biol. , vol.12 , pp. 221-225
    • Gao, L.1
  • 81
    • 0037096161 scopus 로고    scopus 로고
    • Involvement of ASIP/PAR-3 in the promotion of epithelial tight junction formation
    • Hiorose T., et al. Involvement of ASIP/PAR-3 in the promotion of epithelial tight junction formation. J. Cell Sci. 115:2002;2485-2495
    • (2002) J. Cell Sci. , vol.115 , pp. 2485-2495
    • Hiorose, T.1
  • 82
    • 0037106581 scopus 로고    scopus 로고
    • APKC kinase activity is required for the asymmetric differentiation of the premature junctional complex during epithelial cell polarization
    • Suzuki A., et al. aPKC kinase activity is required for the asymmetric differentiation of the premature junctional complex during epithelial cell polarization. J. Cell Sci. 115:2002;3565-3573
    • (2002) J. Cell Sci. , vol.115 , pp. 3565-3573
    • Suzuki, A.1
  • 83
    • 0035898658 scopus 로고    scopus 로고
    • The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)
    • Ebnet K., et al. The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM). EMBO J. 20:2001;3738-3748
    • (2001) EMBO J. , vol.20 , pp. 3738-3748
    • Ebnet, K.1
  • 84
    • 0035817623 scopus 로고    scopus 로고
    • Junctional adhesion molecule (JAM) binds to PAR-3: A possible mechanism for the recruitment of PAR-3 to tight junctions
    • Itoh M., et al. Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions. J. Cell Biol. 154:2001;491-497
    • (2001) J. Cell Biol. , vol.154 , pp. 491-497
    • Itoh, M.1
  • 85
    • 0033790539 scopus 로고    scopus 로고
    • The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1
    • Johansson A., et al. The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1. J. Cell Sci. 113:2000;3267-3275
    • (2000) J. Cell Sci. , vol.113 , pp. 3267-3275
    • Johansson, A.1
  • 86
    • 0034253587 scopus 로고    scopus 로고
    • Cell polarity: New PARtners for Cdc42 and Rac
    • Kim S.K. Cell polarity: new PARtners for Cdc42 and Rac. Nat. Cell Biol. 2:2000;E143-E145
    • (2000) Nat. Cell Biol. , vol.2 , pp. 143-E145
    • Kim, S.K.1
  • 87
    • 0037319350 scopus 로고    scopus 로고
    • Direct interaction of two polarity complexes implicated in epithelial tight junction assembly
    • Hurd T.W., et al. Direct interaction of two polarity complexes implicated in epithelial tight junction assembly. Nat. Cell Biol. 5:2003;137-142
    • (2003) Nat. Cell Biol. , vol.5 , pp. 137-142
    • Hurd, T.W.1
  • 88
    • 0031213571 scopus 로고    scopus 로고
    • Mammalian homologues of C. elegans PAR-1 are asymmetrically localized in epithelial cells and may influence their polarity
    • Bohm H., et al. Mammalian homologues of C. elegans PAR-1 are asymmetrically localized in epithelial cells and may influence their polarity. Curr. Biol. 7:1997;603-606
    • (1997) Curr. Biol. , vol.7 , pp. 603-606
    • Bohm, H.1
  • 89
    • 0037941137 scopus 로고    scopus 로고
    • Apical surface formation in MDCK cells: Regulation by the serine/threonine kinase EMK1
    • Cohen D., Musch A. Apical surface formation in MDCK cells: regulation by the serine/threonine kinase EMK1. Methods. 30:2003;269-276
    • (2003) Methods , vol.30 , pp. 269-276
    • Cohen, D.1    Musch, A.2
  • 90
    • 0344663968 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of 14-3-3 to the polarity protein Par3 regulates cell polarity in mammalian epithelia
    • Hurd T.W., et al. Phosphorylation-dependent binding of 14-3-3 to the polarity protein Par3 regulates cell polarity in mammalian epithelia. Curr. Biol. 13:2003;2082-2090
    • (2003) Curr. Biol. , vol.13 , pp. 2082-2090
    • Hurd, T.W.1
  • 91
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning G., et al. The protein kinase complement of the human genome. Science. 298:2002;1912-1934
    • (2002) Science , vol.298 , pp. 1912-1934
    • Manning, G.1
  • 92
    • 0034640089 scopus 로고    scopus 로고
    • PARsing embryonic polarity
    • Kemphues K. PARsing embryonic polarity. Cell. 101:2000;345-348
    • (2000) Cell , vol.101 , pp. 345-348
    • Kemphues, K.1


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