VIPL, a VIP36-like membrane protein with a putative function in the export of glycoproteins from the endoplasmic reticulum

被引:53
作者
Neve, EPA [1 ]
Svensson, K [1 ]
Fuxe, J [1 ]
Pettersson, RF [1 ]
机构
[1] Ludwig Inst Canc Res, Stockholm Branch, Karolinska Inst, SE-17177 Stockholm, Sweden
关键词
lectin; endoplasmic reticulum; ER export; glycoproteins; ERGIC-53; p58; ERGIC; protein transport; exocytic pathway;
D O I
10.1016/S0014-4827(03)00161-7
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Subsets of glycoproteins are thought to require lectin-like membrane receptors for efficient export out of the endoplasmic reticulum (ER). To identify new members related to two previously characterized intracellular lectins ERGIC-53/p58 and VIP36, we carried out an extensive database search using the conserved carbohydrate recognition domain (CRD) as a search string. A gene, more closely related to VIP36 than to ERGIC-53/p58, and hence called VIPL (VIP36-Like), was identified. VIPL has been conserved through evolution from zebra fish to man. The 2.4-kb VIPL mRNA was widely expressed to varying levels in different tissues. Using an antiserum prepared against the CRD, the 32-kDa VIPL protein was detected in various cell lines. The single N-linked glycan of VIPL remained endoglycosidase H-sensitive during a 2-h pulse-chase, even when the protein was overexpressed or mutated to allow export to the plasma membrane. VIPL localized primarily to the ER and partly to the Golgi complex. Like VIP36, the cytoplasmic tail of VIPL terminates in the sequence KRFY, a motif characteristic for proteins recycling between the ER and ERGIC/cis-Golgi. Mutating the retrograde transport signal KR to AA resulted in transport of VIPL to the cell surface. Finally, knock-down of VIPL mRNA using siRNA significantly slowed down the secretion of two glycoproteins (M-R 35 and 250 kDa) to the medium, suggesting that VIPL may also function as an ER export receptor. (C) 2003 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:70 / 83
页数:14
相关论文
共 60 条
[51]   Lectin control of protein folding and sorting in the secretory pathway [J].
Schrag, JD ;
Procopio, DO ;
Cygler, M ;
Thomas, DY ;
Bergeron, JJM .
TRENDS IN BIOCHEMICAL SCIENCES, 2003, 28 (01) :49-57
[52]   THE GOLGI-LOCALIZATION OF YEAST EMP47P DEPENDS ON ITS DI-LYSINE MOTIF BUT IS NOT AFFECTED BY THE RET1-1 MUTATION IN ALPHA-COP [J].
SCHRODER, S ;
SCHIMMOLLER, F ;
SINGERKRUGER, B ;
RIEZMAN, H .
JOURNAL OF CELL BIOLOGY, 1995, 131 (04) :895-912
[53]   IDENTIFICATION, BY A MONOCLONAL-ANTIBODY, OF A 53-KD PROTEIN ASSOCIATED WITH A TUBULO-VESICULAR COMPARTMENT AT THE CIS-SIDE OF THE GOLGI-APPARATUS [J].
SCHWEIZER, A ;
FRANSEN, JAM ;
BACHI, T ;
GINSEL, L ;
HAURI, HP .
JOURNAL OF CELL BIOLOGY, 1988, 107 (05) :1643-1653
[54]   Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs [J].
Sevier, CS ;
Weisz, OA ;
Davis, M ;
Machamer, CE .
MOLECULAR BIOLOGY OF THE CELL, 2000, 11 (01) :13-22
[55]   The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae [J].
Springer, S ;
Chen, E ;
Duden, R ;
Marzioch, M ;
Rowley, A ;
Hamamoto, S ;
Merchant, S ;
Schekman, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (08) :4034-4039
[56]   Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum [J].
Velloso, LM ;
Svensson, K ;
Schneider, G ;
Pettersson, RF ;
Lindqvist, Y .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (18) :15979-15984
[57]   Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme [J].
Vollenweider, F ;
Kappeler, F ;
Itin, C ;
Hauri, HP .
JOURNAL OF CELL BIOLOGY, 1998, 142 (02) :377-389
[58]   THE RATE OF BULK FLOW FROM THE ENDOPLASMIC-RETICULUM TO THE CELL-SURFACE [J].
WIELAND, FT ;
GLEASON, ML ;
SERAFINI, TA ;
ROTHMAN, JE .
CELL, 1987, 50 (02) :289-300
[59]   ERGL, a novel gene related to ERGIC-53 that is highly expressed in normal and neoplastic prostate and several other tissues [J].
Yerushalmi, N ;
Keppler-Hafkemeyer, A ;
Vasmatzis, G ;
Liu, XF ;
Olsson, P ;
Bera, TK ;
Duray, P ;
Lee, B ;
Pastan, I .
GENE, 2001, 265 (1-2) :55-60
[60]   A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane KATP channels [J].
Zerangue, N ;
Schwappach, B ;
Jan, YN ;
Jan, LY .
NEURON, 1999, 22 (03) :537-548