Lipid modifications of proteins -: slipping in and out of membranes

被引:80
作者
Yalovsky, S [1 ]
Rodríguez-Concepción, M [1 ]
Gruissem, W [1 ]
机构
[1] Univ Calif Berkeley, Dept Plant & Microbial Biol, Berkeley, CA 94720 USA
关键词
D O I
10.1016/S1360-1385(99)01492-2
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Protein lipid modification, once thought to act as a stable membrane anchor for soluble proteins, is now attracting more widespread attention for its emerging role in diverse signaling pathways and regulatory mechanisms. Most multicellular organisms have recruited specific types of lipids and a suite of unique enzymes to catatyze the modification of a select number of proteins, many of which are evolutionarily conserved in plants, animals and fungi. Each of the three known types of lipid modification - palmitoylation, myristylation and prenylation - allows cells to target proteins to the plasma membrane, as well as to other subcellular compartments. Among the lipid modifications, protein prenylation might also function as a relay between cytoplasmic isoprene biosynthesis and regulatory pathways that control cell cycle and growth, Molecular and genetic studies of an Arabidopsis mutant that tacks farnesyl transferase suggest that the enzyme has a role in abscisic acid signaling during seed germination and in the stomata. it is becoming clear that lipid modifications are not just fat for the protein, but part of a highly conserved intricate network that plays a role in coordinating complex cellular functions.
引用
收藏
页码:439 / 445
页数:7
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  • [1] Molecular mechanics of calcium-myristoyl switches
    Ames, JB
    Ishima, R
    Tanaka, T
    Gordon, JI
    Stryer, L
    Ikura, M
    [J]. NATURE, 1997, 389 (6647) : 198 - 202
  • [2] Understanding covalent modifications of proteins by lipids: Where cell biology and biophysics mingle
    Bhatnagar, RS
    Gordon, JI
    [J]. TRENDS IN CELL BIOLOGY, 1997, 7 (01) : 14 - 20
  • [3] BIERMANN BJ, 1994, J BIOL CHEM, V269, P25251
  • [4] A non-farnesylated Ha-Ras protein can be palmitoylated and trigger potent differentiation and transformation
    Booden, MA
    Baker, TL
    Solski, PA
    Der, CJ
    Punke, SG
    Buss, JE
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (03) : 1423 - 1431
  • [5] CHAPPELL J, 1995, PLANT PHYSIOL, V107, P1, DOI 10.1145/224057.224059
  • [6] Endomembrane trafficking of Ras: The CAAX motif targets proteins to the ER and Golgi
    Choy, E
    Chiu, VK
    Silletti, J
    Feoktistov, M
    Morimoto, T
    Michaelson, D
    Ivanov, IE
    Philips, MR
    [J]. CELL, 1999, 98 (01) : 69 - 80
  • [8] Prenylcysteine α-carboxyl methyltransferase in suspension-cultured tobacco cells
    Crowell, DN
    Sen, SE
    Randall, SK
    [J]. PLANT PHYSIOLOGY, 1998, 118 (01) : 115 - 123
  • [9] A protein farnesyl transferase involved in abscisic acid signal transduction in Arabidopsis
    Cutler, S
    Ghassemian, M
    Bonetta, D
    Cooney, S
    McCourt, P
    [J]. SCIENCE, 1996, 273 (5279) : 1239 - 1241
  • [10] Post-translational modification of human brain type I inositol-1,4,5-trisphosphate 5-phosphatase by farnesylation
    DeSmedt, F
    Boom, A
    Pesesse, X
    Schiffmann, SN
    Erneux, C
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (17) : 10419 - 10424