title: The Sur7 protein regulates plasma membrane organization and prevents intracellular cell wall growth in Candida albicans.
abstract: The Candida albicans plasma membrane plays important roles in cell growth and as a target for antifungal drugs. Analysis of Ca-Sur7 showed that this four transmembrane domain protein localized to stable punctate patches, similar to the plasma membrane subdomains known as eisosomes or MCC that were discovered in S. cerevisiae. The localization of Ca-Sur7 depended on sphingolipid synthesis. In contrast to S. cerevisiae, a C. albicans sur7Delta mutant displayed defects in endocytosis and morphogenesis. Septins and actin were mislocalized, and cell wall synthesis was very abnormal, including long projections of cell wall into the cytoplasm. Several phenotypes of the sur7Delta mutant are similar to the effects of inhibiting beta-glucan synthase, suggesting that the abnormal cell wall synthesis is related to activation of chitin synthase activity seen under stress conditions. These results expand the roles of eisosomes by demonstrating that Sur7 is needed for proper plasma membrane organization and cell wall synthesis. A conserved Cys motif in the first extracellular loop of fungal Sur7 proteins is similar to a characteristic motif of the claudin proteins that form tight junctions in animal cells, suggesting a common role for these tetraspanning membrane proteins in forming specialized plasma membrane domains.
authors.affiliation: Department of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY 11794-5222, USA.
authors.forename: Francisco J
authors.initials: FJ
authors.lastname: Alvarez
authors.forename: Lois M
authors.initials: LM
authors.lastname: Douglas
authors.forename: Adam
authors.initials: A
authors.lastname: Rosebrock
authors.forename: James B
authors.initials: JB
authors.lastname: Konopka
mesh_terms: D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D002176:Candida albicans / Q000166:cytology* / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D002473:Cell Wall / Q000502:physiology* / Q000648:ultrastructure; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism; D004705:Endocytosis / Q000502:physiology; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D020869:Gene Expression Profiling; D006801:Humans; D025301:Hyphae / Q000502:physiology / Q000648:ultrastructure; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009024:Morphogenesis; D020411:Oligonucleotide Array Sequence Analysis; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D000199:Actins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D005656:Fungal Proteins; C487328:LSP1 protein, S cerevisiae; D008565:Membrane Proteins; D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins; C502213:SUR7 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins
references.citation: J Biol Chem. 2000 Jun 9;275(23):17221-4
references.pmid: 10770957
references.citation: PLoS Pathog. 2008 Apr 04;4(4):e1000040
references.pmid: 18389063
references.citation: Methods Enzymol. 1991;194:3-21
references.pmid: 2005794
references.citation: Trends Microbiol. 2004 Jul;12(7):317-24
references.pmid: 15223059
references.citation: Curr Opin Cell Biol. 2004 Apr;16(2):140-5
references.pmid: 15196556
references.citation: Nature. 2002 Jan 10;415(6868):141-7
references.pmid: 11805826
references.citation: Yeast. 1997 Jun 30;13(8):747-61
references.pmid: 9219339
references.citation: Mol Cell. 2000 May;5(5):841-51
references.pmid: 10882120
references.citation: Mol Biol Cell. 2002 Aug;13(8):2732-46
references.pmid: 12181342
references.citation: Mol Biol Cell. 2006 Aug;17(8):3409-22
references.pmid: 16738305
references.citation: Trends Microbiol. 2003 Jun;11(6):272-9
references.pmid: 12823944
references.citation: Methods Enzymol. 1991;194:729-31
references.pmid: 2005819
references.citation: Antimicrob Agents Chemother. 2004 Nov;48(11):4491
references.pmid: 15504893
references.citation: Eukaryot Cell. 2005 Sep;4(9):1503-12
references.pmid: 16151244
references.citation: J Cell Sci. 2006 Nov 15;119(Pt 22):4585-7
references.pmid: 17093262
references.citation: Nature. 2003 Oct 16;425(6959):686-91
references.pmid: 14562095
references.citation: Microbiology (Reading). 2005 Jul;151(Pt 7):2241-2249
references.pmid: 16000714
references.citation: Prog Lipid Res. 2006 Nov;45(6):447-65
references.pmid: 16730802
references.citation: Mol Biol Cell. 2002 Aug;13(8):2747-59
references.pmid: 12181343
references.citation: Mol Biol Cell. 2003 May;14(5):2128-41
references.pmid: 12802080
references.citation: Physiology (Bethesda). 2004 Dec;19:331-8
references.pmid: 15546850
references.citation: Mol Biol Cell. 2007 Mar;18(3):965-75
references.pmid: 17192409
references.citation: Methods Enzymol. 1991;194:732-5
references.pmid: 2005820
references.citation: Curr Opin Microbiol. 2001 Dec;4(6):681-9
references.pmid: 11731320
references.citation: Yeast. 1998 Jul;14(10):953-61
references.pmid: 9717241
references.citation: J Cell Sci. 2004 Dec 1;117(Pt 25):6031-41
references.pmid: 15536122
references.citation: Science. 2000 Oct 13;290(5490):341-4
references.pmid: 11030653
references.citation: Nat Rev Mol Cell Biol. 2005 Oct;6(10):801-11
references.pmid: 16314869
references.citation: Nature. 2006 Feb 23;439(7079):998-1003
references.pmid: 16496001
references.citation: Eukaryot Cell. 2006 Oct;5(10):1726-37
references.pmid: 17030998
references.citation: FEBS Lett. 2000 Jul 28;478(1-2):84-8
references.pmid: 10922474
references.citation: J Biol Chem. 2003 Oct 3;278(40):38461-9
references.pmid: 12878605
references.citation: J Cell Biol. 1995 Mar;128(5):779-92
references.pmid: 7533169
references.citation: Microbiology (Reading). 2001 Apr;147(Pt 4):781-794
references.pmid: 11283274
references.citation: EMBO J. 2007 Dec 12;26(24):4946-55
references.pmid: 18034155
references.citation: Mol Biol Cell. 2003 Nov;14(11):4427-36
references.pmid: 14551254
references.citation: Yeast. 1999 Apr;15(6):507-11
references.pmid: 10234788
references.citation: Annu Rev Physiol. 2006;68:403-29
references.pmid: 16460278
references.citation: Trends Cell Biol. 2003 Aug;13(8):403-9
references.pmid: 12888292
references.citation: Eukaryot Cell. 2004 Jun;3(3):675-84
references.pmid: 15189988
references.citation: Nat Rev Microbiol. 2006 Mar;4(3):223-9
references.pmid: 16429163
references.citation: Trends Cell Biol. 2006 Apr;16(4):181-8
references.pmid: 16537104
references.citation: Mol Cell Biol. 2002 Feb;22(3):927-34
references.pmid: 11784867
references.citation: Eukaryot Cell. 2007 May;6(5):755-63
references.pmid: 17369440
references.citation: J Biol Chem. 2008 Apr 18;283(16):10433-44
references.pmid: 18296441
references.citation: Yeast. 2001 Jun 30;18(9):859-64
references.pmid: 11427968
references.citation: PLoS Pathog. 2006 Mar;2(3):e21
references.pmid: 16552442
references.citation: Nat Cell Biol. 2003 Jul;5(7):626-32
references.pmid: 12819789
references.citation: J Lipid Res. 2008 May;49(5):909-21
references.pmid: 18296751
references.citation: J Bacteriol. 1999 Mar;181(6):1868-74
references.pmid: 10074081
references.citation: Yeast. 2000 Jan 15;16(1):65-70
references.pmid: 10620776
references.citation: Antimicrob Agents Chemother. 1998 May;42(5):1187-94
references.pmid: 9593148
references.citation: Nucleic Acids Res. 1994 Nov 11;22(22):4673-80
references.pmid: 7984417
references.citation: Cell. 1992 Nov 27;71(5):755-63
references.pmid: 1330324
references.citation: EMBO J. 2007 Jan 10;26(1):1-8
references.pmid: 17170709
references.citation: J Mol Biol. 1990 Oct 5;215(3):403-10
references.pmid: 2231712