14-3-3 Proteins Form a Guidance Complex with Chloroplast Precursor Proteins in Plants
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چکیده
منابع مشابه
14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants.
Transit sequences of chloroplast-destined precursor proteins are phosphorylated on a serine or threonine residue. The amino acid motif around the phosphorylation site is related to the phosphopeptide binding motif for 14-3-3 proteins. Plant 14-3-3 proteins interact specifically with wheat germ lysate-synthesized chloroplast precursor proteins and require an intact phosphorylation motif within t...
متن کاملThe 14-3-3 proteins
So what’s so interesting about them? In 1996 14-3-3 was found to bind to a variety of oncoproteins including Raf-1, polyoma middle T, and Bcr-Abl. Since then the 14-3-3 proteins have been shown to bind to a wide variety of proteins involved in signal transduction, cell cycle and apoptosis. These proteins include Cdc25, NFAT, Bad, Cbl, A20, PI 3-kinase, IRS-1, MEKK, p130Cas, glucocorticoid recep...
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The once obscure members of the 14-3-3 protein family play significant roles in the determination of cell fate. By inhibiting the pro-apoptotic BAD (Bcl-2-antagonist of cell death) and the transcription factor FKHRL-1, 14-3-3 displays important anti-apoptotic characteristics. To date, five points of interaction of 14-3-3 with the apoptotic machinery have been identified. How these interactions ...
متن کامل14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner.
Recently, we have demonstrated by two different methods that lipoxgenases (LOXs) and 14-3-3 proteins form interactions in barley embryos [Holtman, Roberts, Oppedijk, Testerink, van Zeijl and Wang (2000) FEBS Lett. 474, 48-52]. It was shown by both co-immunoprecipitations and surface-plasmon resonance experiments that 13-LOX, but not 9-LOX, forms interactions with 14-3-3 proteins. In the present...
متن کامل14-3-3 Proteins Interact with a Hybrid Prenyl-Phosphorylation Motif to Inhibit G Proteins
Signaling through G proteins normally involves conformational switching between GTP- and GDP-bound states. Several Rho GTPases are also regulated by RhoGDI binding and sequestering in the cytosol. Rnd proteins are atypical constitutively GTP-bound Rho proteins, whose regulation remains elusive. Here, we report a high-affinity 14-3-3-binding site at the C terminus of Rnd3 consisting of both the ...
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ژورنال
عنوان ژورنال: The Plant Cell
سال: 2000
ISSN: 1040-4651,1532-298X
DOI: 10.1105/tpc.12.1.53