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2013 | 60 | 1 |
Tytuł artykułu

Vps41, a protein involved in lysosomal trafficking, interacts with caspase-8

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Języki publikacji
EN
Abstrakty
EN
 Caspase-8 is a member of the cysteine-aspartic acid protease (caspase) family which plays a central role in apoptosis and development. We screened caspase-8 interacting proteins from mouse T-cell lymphoma and 7.5-day embryo cDNA libraries by yeast two-hybrid system and obtained eleven positive clones, including Vacuolar protein sorting 41 (Vps41), a protein involved in trafficking of proteins from the late Golgi to the vacuole. The interaction of Vps41 with caspase-8 was confirmed by co-immunoprecipitation (co-IP) and co-localization studies in HEK293T cells. Co-IP experiments also showed that Vps41 binds to the p18 subunit of caspase-8 through its WD40 region and RING-finger motif. Furthermore, we found that overexpression of Vps41 promotes Fas-induced apoptosis in A549 human lung adenocarcinoma cells. The cleavage of caspase-3, a caspase-8 downstream effector, was increased when cells were transfected with Vps41-overexpressing plasmid. Together, these results suggest a novel interaction of caspase-8 with Vps41 and provide a potential role of Vps41 beyond lysosomal trafficking.
Słowa kluczowe
Wydawca
-
Rocznik
Tom
60
Numer
1
Opis fizyczny
p.37-42,fig.,ref.
Twórcy
autor
  • The State Key Laboratory of Pharmaceutical Biotechnology and School of Stomatology, Affiliated Stomatological Hospital, Nanjing University, Nanjing, PR China
autor
  • The State Key Laboratory of Pharmaceutical Biotechnology and School of Stomatology, Affiliated Stomatological Hospital, Nanjing University, Nanjing, PR China
autor
  • The State Key Laboratory of Pharmaceutical Biotechnology and School of Stomatology, Affiliated Stomatological Hospital, Nanjing University, Nanjing, PR China
autor
  • The State Key Laboratory of Pharmaceutical Biotechnology and School of Stomatology, Affiliated Stomatological Hospital, Nanjing University, Nanjing, PR China
autor
  • The State Key Laboratory of Pharmaceutical Biotechnology and School of Stomatology, Affiliated Stomatological Hospital, Nanjing University, Nanjing, PR China
autor
  • The State Key Laboratory of Pharmaceutical Biotechnology and School of Stomatology, Affiliated Stomatological Hospital, Nanjing University, Nanjing, PR China
autor
  • The State Key Laboratory of Pharmaceutical Biotechnology and School of Stomatology, Affiliated Stomatological Hospital, Nanjing University, Nanjing, PR China
  • Changzhou High-Tech Research Institute of Nanjing University, Changzhou, P. R. China.
autor
  • The State Key Laboratory of Pharmaceutical Biotechnology and School of Stomatology, Affiliated Stomatological Hospital, Nanjing University, Nanjing, PR China
  • Changzhou High-Tech Research Institute of Nanjing University, Changzhou, P. R. China.
Bibliografia
  • An CH, Kim YR, Kim HS, Kim SS, Yoo NJ, Lee SH (2012) Frameshift mutations of vacuolar protein sorting genes in gastric and colorectal cancers with microsatellite instability. Hum Pathol 43: 40-47. 
  • Boldin MP, Goncharov TM, Goltsev YV, Wallach D (1996) Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 85: 803-815. 
  • Bossy-Wetzel E, Newmeyer DD, Green DR (1998) Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J 17: 37-49. 
  • Bratton SB, MacFarlane M, Cain K, Cohen GM (2000) Protein complexes activate distinct caspase cascades in death receptor and stress-induced apoptosis. Exp Cell Res 256: 27-33. 
  • Brett CL, Plemel RL, Lobingier BT, Vignali M, Fields S, Merz AJ (2008) Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase. J Cell Biol 182: 1141-1151. 
  • Cabrera M, Langemeyer L, Mari M, Rethmeier R, Orban I, Perz A, Bröcker C, Griffith J, Klose D, Steinhoff HJ, Reggiori F, Engelbrecht-Vandré S, Ungermann C (2010) Phosphorylation of a membrane curvature-sensing motif switches function of the HOPS subunit Vps41 in membrane tethering. J Cell Biol 191: 845-859. 
  • Cohen GM (1997) Caspases: the executioners of apoptosis. Biochem J 326: 1-16. 
  • Conibear E, Stevens TH (1998) Multiple sorting pathways between the late Golgi and the vacuole in yeast. Biochim Biophys Acta 1404: 211-230. 
  • Fischer B, Coelho D, Dufour P, Bergerat JP, Denis JM, Gueulette J, Bischoff P (2003) Caspase 8-mediated cleavage of the pro-apoptotic BCL-2 family member BID in p53-dependent apoptosis. Biochem Biophys Res Commun 306: 516-522. 
  • Garg S, Sharma M, Ung C, Tuli A, Barral DC, Hava DL, Veerapen N, Besra GS, Hacohen N, Brenner MB (2011) Lysosomal trafficking, antigen presentation, and microbial killing are controlled by the Arf-like GTPase Arl8b. Immunity 35: 182-193. 
  • Harrington AJ, Yacoubian TA, Slone SR, Caldwell KA, Caldwell GA (2012) Functional analysis of VPS41-mediated neuroprotection in Caenorhabditis elegans and mammalian models of Parkinson's disease. J Neurosci 32: 2142-2153. 
  • Juo P, Kuo CJ, Yuan J, Blenis J (1998) Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade. Curr Biol 8: 1001-1008. 
  • Li H, Zhu H, Xu CJ, Yuan J (1998) Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94: 491-501. 
  • McVey Ward D, Radisky D, Scullion MA, Tuttle MS, Vaughn M, Kaplan J (2001) hVPS41 Is Expressed in Multiple Isoforms and Can Associate with Vesicles through a RING-H2 Finger Motif. Exp Cell Res 267: 126-134. 
  • Mellman I, Warren G (2000) The road taken: past and future foundations of membrane traffic. Cell 100: 99-112. 
  • Muzio M, Chinnaiyan AM, Kischkel FC, O'Rourke K, Shevchenko A, Ni J, Scaffidi C, Bretz JD, Zhang M, Gentz R, Mann M, Krammer PH, Peter ME, Dixit VM (1996) FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 85: 817-827. 
  • Radisky DC, Snyder WB, Emr SD, Kaplan J (1997) Characterization of VPS41, a gene required for vacuolar trafficking and high-affinity iron transport in yeast. Proc Natl Acad Sci USA 94: 5662-5666. 
  • Rehling P, Darsow T, Katzmann DJ, Emr SD (1999) Formation of AP-3 transport intermediates requires Vps41 function. Nat Cell Biol 1: 346-353. 
  • Roy D, Sin SH, Damania B, Dittmer DP (2011) Tumor suppressor genes FHIT and WWOX are deleted in primary effusion lymphoma (PEL) cell lines. Blood 118: e32-e39. 
  • Ruan Q, Harrington AJ, Caldwell KA, Caldwell GA, Standaert DG (2010) VPS41, a protein involved in lysosomal trafficking, is protective in Caenorhabditis elegans and mammalian cellular models of Parkinson's disease. Neurobiol Dis 37: 330-338. 
  • Wurmser AE, Sato TK, Emr SD (2000) New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion. J Cell Biol 151: 551-562. 
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