Cab45, a novel Ca2+-binding protein localized to the Golgi lumen

Journal of Cell Biology

Volumn 133, Issue 2, 1996, Pages 257-268

  Scherer, Philipp E ^a   Lederkremer, Gerardo Z ^b   Williams, Suzanne ^c   Fogliano, Michael ^c   Baldini, Giulia ^a,d   Lodish, Harvey F ^a  

^a WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

^b TEL AVIV UNIVERSITY   (Israel)

^c PFIZER GLOBAL RESEARCH AND DEVELOPMENT   (United States)

^d The New York Presbyterian Hospital   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BREFELDIN A; CAB45 PROTEIN, HUMAN; CALCIUM BINDING PROTEIN; COMPLEMENTARY DNA; CYCLOPENTANE DERIVATIVE; GLYCOPROTEIN; HYBRID PROTEIN; MESSENGER RNA; PROTEIN SYNTHESIS INHIBITOR; CALCIUM 45; CALCIUM BINDING PROTEIN CAB 45; CALCIUM ION; UNCLASSIFIED DRUG;

ADIPOCYTE; AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CELL STRAIN 3T3; CHEMISTRY; DNA SEQUENCE; GENE EXPRESSION; GENETICS; GLYCOSYLATION; GOLGI COMPLEX; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; MOLECULAR WEIGHT; MOUSE; NUCLEOTIDE SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; CALCIUM BINDING; ENDOPLASMIC RETICULUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION;

3T3 CELLS; ADIPOCYTES; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BREFELDIN A; CALCIUM-BINDING PROTEINS; CLONING, MOLECULAR; CYCLOPENTANES; DNA, COMPLEMENTARY; GENE EXPRESSION; GLYCOPROTEINS; GLYCOSYLATION; GOLGI APPARATUS; MICE; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PROTEIN SYNTHESIS INHIBITORS; RECOMBINANT FUSION PROTEINS; RNA, MESSENGER; SEQUENCE ANALYSIS, DNA;

EID: 0029664786     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.133.2.257     Document Type: Article

References (36)

1. Amara, J.F., G. Lederkremer, and H.F. Lodish 1989. Intracellular degradation of unassembled asialoglycoprotein receptor subumts: a pre-Golgi, nonlysosomal endoproteolytic cleavage. J Cell Biol 109:3315-3324.
2. Andres, D.A., I.M. Dickerson, and J.E. Dixon. 1990 Variants of the carboxylterminal KDEL sequence direct intracellular retention. J. Biol. Chem. 265: 5952-5955.
3. Andres, D A., J D. Rhodes, R.L. Meisel, and J.E. Dixon. 1991. Characterization of the carboxyl-terminal sequences responsible for protein retention in the endoplasmic reticuium. J. Biol. Chem. 266:14277-14282.
4. Baldini, G , T. Hohl, H.Y Lin, and H.F. Lodish 1992. Cloning of a Rab3 isotype predominantly expressed in adipocytes. Proc. Natl. Acad. Sci. USA 89. 5049-5052.
5. Bole, D.O., L.M. Hendershot. and J F. Kearney. 1986. Posttranslational association of imimunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J. Cell Biol. 102:1558-1566.
6. Edman, J.C., L. Ellis, R.W. Blacher, R.A. Roth, and W J. Rutter. 1985. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature (Lond.). 317:267-270.
7. Frost. S.C., and M.D. Lane. 1985. Evidence for the involvement of vicinal sulfhydryl groups in insulin-activated hexose transport by 3T3-L1 adipocytes. J. Biol. Chem. 260:2646-2652.
8. Fujiki, Y., A.L. Hubbard, S. Fowler, and P.B. Lazarow. 1982. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:97-102
9. Harlow, E., and D. Lane. 1988. Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor. NY.
10. Heizmann, C.W., and W. Hunziker. 1991. Intracellular calcium-binding proteins: more sites than insights. Trends Biochem. Sci 16:98-103.
11. Hunt, C., and S. Calderwood. 1990. Characterization and sequence of a mouse hsp70 gene and its expression in mouse cell lines. Gene. 87:199-204.
12. Itin, C., R. Schindler, and H.-P. Hauri 1995. Targeting of Protein ERGIC-53 to the ER/ERGIC/cis-Golgi recycling pathway. J. Cell Biol. 131:57-67.
13. Kozak, M. 1991. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 266:19867-19870.
14. Kretsinger, R.H., and C.E. Nockolds. 1973. Carp muscle calcium-binding protein. II. Structure determination and general description. J. Biol. Chem 248. 3313-3326.
15. Lippincott-Schwartz., J , J G Donaldson, A. Schweizer, E G. Berger, H.-P. Hauri, L C. Yuan, and R.D. Klausner. 1990. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway Cell. 60:821-836.
16. Lippincott-Schwartz, J., L.C. Yuan, J.S. Bonifacino, and R D. Klausner 1989. Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from the Golgi to ER. Cell. 56: 801-813.
17. Lodish, H.F., N Kong, and L. Wikstrom 1992. Calcium is required for folding of newly made subumts of the asialoglycoprotein receptor within the endoplasmic reticulum. J. Biol. Chem. 267:12753-12760.
18. Lotti, L.V., M-R. Torrisi, M.C. Pascale, and S. Bonatti. 1992. Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex. J. Cell Biol. 118:43-50.
19. Louvard, D., H. Reggio, and G. Warren. 1982 Antibodies to the Golgi complex and the rough endoplasimc reticulum. J. Cell Biol. 92:92-107.
20. 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis J. Biochem. 95:511-519
21. Mazzarella, R.A., and M. Green 1987. ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94). J Biol. Chem. 262:8875-8883.
22. Moremen, K.W , and P.W Robbins. 1991. Isolation, characterization, and expression of cDNAs encoding murine α-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans. J. Cell Biol 115: 1521-1534.
23. Munro, S., and H.R. Pelham. 1986. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell. 46:291-300.
24. Munro, S , and H.R Pelham. 1987. A C-terminal signal prevents secretion of Iuminal ER proteins. Cell. 48:899-907.
25. 2+-binding protein with multiple EF-hand motifs and a carboxy-terminal HDEL sequence J Biol. Chem 268 699-705.
26. Scherer, P.E., M.P. Lisant, G. Baldini. M Sargiacomo, C. Corley-Mastick, and H.F. Lodish. 1994, Induction of caveolin during adipogenesis and association of GLUT4 with caveolin-rich vesicles. J. Cell Biol. 127:1233-1243.
27. Schweizer, A., J.A.M. Fransen, T. Bachi, L Ginsel, and H.-P Hauri. 1988. 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. Cell Biol 108:1643-1653.
28. Schweizer, A., J.A.M. Fransen, K. Matter, T.E. Kreis, L. Ginsel, and H.-P. Hauri. 1990. Identification of an intermediate compartment involved in protein transport from the ER to the Golgi apparatus. Eur J. Cell Biol. 53:185-196.
29. Seed, B., and A. Aruffo 1987. Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure. Proc. Natl. Acad. Sci. USA. 84:3365-3369.
30. Sorger, P.K., and H.R. Pelham. 1987. The glucose-regulated protein grp94 is related to heat shock protein hsp90 J. Mol. Biol. 194:341-344.
31. Suzuki, C K., J.S Borufacino, A.Y. Lin, M.M. Davis. and R.D. Klausner. 1991 Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP. J. Cell Biol 114:189-205.
32. Wada, I., D. Rindress, P.H. Cameron, W.J. Ou, J.J. Doherty, D. Louvard, A.W Bell, D. Dignard. D.Y. Thomas, and J.J. Bergeron 1991. SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J. Biol Chem. 266:19599-19610.
33. Wallace, R.W., E.A. Tallant, and W.Y. Cheung. 1982. Multifunctional role of calmodulin in biologic processes. Cold Spring Harb. Symp. Quant. Biol. 46: 893-901.
34. Weinstein, H., and E.L. Mehler. 1994. Ca(2+)-binding and structural dynamics in the functions of calmodulin. Annu. Rev. Physiol 56:213-236
35. Weis, K., G. Griffiths, and A.I Lamond. 1994 The endoplasmic reticulum calcium-binding protein of 5SkDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxy-terrmnal His-Asp-Glu-Leu motif. J. Biol. Chem. 269:19142-19150.
36. Wileman, T., L.P. Kane, G R. Carson, and C. Terhorst. 1991 Depletion of cellular calcium accelerates protein degradation in the endoplasmic reticulum. J. Biol. Chem. 266:4500-4507