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N-myristoylated proteins, key components in intracellular signal transduction systems enabling rapid and flexible cell responses.

Hayashi N, Titani K - Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. (2010)

Bottom Line: Thus, it has been shown that myristoylated proteins in cells regulate the signal transduction between membranes and cytoplasmic fractions.Interestingly, a large portion of the myristoylated proteins thought to take part in signal transduction between membranes and cytoplasmic fractions are included in the predicted myristoylated proteins.On the basis of our recent results, this review will highlight the multifunctional aspects of protein N-myristoylation in brain.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Science, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama-shi, Kanagawa Pref., 226-8501, Japan. nhayashi@bio.titech.ac.jp

ABSTRACT
N-myristoylation, one of the co- or post-translational modifications of proteins, has so far been regarded as necessary for anchoring of proteins to membranes. Recently, we have revealed that N(alpha)-myristoylation of several brain proteins unambiguously regulates certain protein-protein interactions that may affect signaling pathways in brain. Comparison of the amino acid sequences of myristoylated proteins including those in other organs suggests that this regulation is involved in signaling pathways not only in brain but also in other organs. Thus, it has been shown that myristoylated proteins in cells regulate the signal transduction between membranes and cytoplasmic fractions. An algorithm we have developed to identify myristoylated proteins in cells predicts the presence of hundreds of myristoylated proteins. Interestingly, a large portion of the myristoylated proteins thought to take part in signal transduction between membranes and cytoplasmic fractions are included in the predicted myristoylated proteins. If the proteins functionally regulated by myristoylation, a posttranslational protein modification, were understood as cross-talk points within the intracellular signal transduction system, known signaling pathways could thus be linked to each other, and a novel map of this intracellular network could be constructed. On the basis of our recent results, this review will highlight the multifunctional aspects of protein N-myristoylation in brain.

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Related in: MedlinePlus

Titration of Ca2+/CaM with mC/N9 studied by CaM uniformly labeled with 15N and 1H-15N HSQC NMR spectroscopy. The sample contained 0.5 mM CaM, 120 mM NaCl, 2.5 mM CaCl2, and 50 mM deuterated TrisHCl (pH 7.5) in 90% H2O and 10% D2O. The resonance assignments were made with reference to Ikura et al.83) The three well isolated regions are indicated. The tentative assignments (Lys21, Ile27, Ala57) are shown. The spectra of Ca2+/CaM in the presence of 0, 1, 2, 3, 4 and 5 molar equivalents of mC/N9 are shown by the number, respectively.
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fig07: Titration of Ca2+/CaM with mC/N9 studied by CaM uniformly labeled with 15N and 1H-15N HSQC NMR spectroscopy. The sample contained 0.5 mM CaM, 120 mM NaCl, 2.5 mM CaCl2, and 50 mM deuterated TrisHCl (pH 7.5) in 90% H2O and 10% D2O. The resonance assignments were made with reference to Ikura et al.83) The three well isolated regions are indicated. The tentative assignments (Lys21, Ile27, Ala57) are shown. The spectra of Ca2+/CaM in the presence of 0, 1, 2, 3, 4 and 5 molar equivalents of mC/N9 are shown by the number, respectively.

Mentions: We analyzed the interaction between mC/N9 and Ca2+/CaM using 15N labeled CaM and two-dimensional 1H-15N HSQC NMR spectroscopy. Portions of the NMR spectra for Ca2+/CaM in the absence or presence of mC/N9 are shown in Fig. 7. When mC/N9 was added, shifts of certain peaks were observed in the 1H-15N HSQC NMR spectra of Ca2+/CaM. Some drastic shifts of the peaks were also observed by addition of 2 molar equivalents of mC/N9.


N-myristoylated proteins, key components in intracellular signal transduction systems enabling rapid and flexible cell responses.

Hayashi N, Titani K - Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. (2010)

Titration of Ca2+/CaM with mC/N9 studied by CaM uniformly labeled with 15N and 1H-15N HSQC NMR spectroscopy. The sample contained 0.5 mM CaM, 120 mM NaCl, 2.5 mM CaCl2, and 50 mM deuterated TrisHCl (pH 7.5) in 90% H2O and 10% D2O. The resonance assignments were made with reference to Ikura et al.83) The three well isolated regions are indicated. The tentative assignments (Lys21, Ile27, Ala57) are shown. The spectra of Ca2+/CaM in the presence of 0, 1, 2, 3, 4 and 5 molar equivalents of mC/N9 are shown by the number, respectively.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3108300&req=5

fig07: Titration of Ca2+/CaM with mC/N9 studied by CaM uniformly labeled with 15N and 1H-15N HSQC NMR spectroscopy. The sample contained 0.5 mM CaM, 120 mM NaCl, 2.5 mM CaCl2, and 50 mM deuterated TrisHCl (pH 7.5) in 90% H2O and 10% D2O. The resonance assignments were made with reference to Ikura et al.83) The three well isolated regions are indicated. The tentative assignments (Lys21, Ile27, Ala57) are shown. The spectra of Ca2+/CaM in the presence of 0, 1, 2, 3, 4 and 5 molar equivalents of mC/N9 are shown by the number, respectively.
Mentions: We analyzed the interaction between mC/N9 and Ca2+/CaM using 15N labeled CaM and two-dimensional 1H-15N HSQC NMR spectroscopy. Portions of the NMR spectra for Ca2+/CaM in the absence or presence of mC/N9 are shown in Fig. 7. When mC/N9 was added, shifts of certain peaks were observed in the 1H-15N HSQC NMR spectra of Ca2+/CaM. Some drastic shifts of the peaks were also observed by addition of 2 molar equivalents of mC/N9.

Bottom Line: Thus, it has been shown that myristoylated proteins in cells regulate the signal transduction between membranes and cytoplasmic fractions.Interestingly, a large portion of the myristoylated proteins thought to take part in signal transduction between membranes and cytoplasmic fractions are included in the predicted myristoylated proteins.On the basis of our recent results, this review will highlight the multifunctional aspects of protein N-myristoylation in brain.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Science, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama-shi, Kanagawa Pref., 226-8501, Japan. nhayashi@bio.titech.ac.jp

ABSTRACT
N-myristoylation, one of the co- or post-translational modifications of proteins, has so far been regarded as necessary for anchoring of proteins to membranes. Recently, we have revealed that N(alpha)-myristoylation of several brain proteins unambiguously regulates certain protein-protein interactions that may affect signaling pathways in brain. Comparison of the amino acid sequences of myristoylated proteins including those in other organs suggests that this regulation is involved in signaling pathways not only in brain but also in other organs. Thus, it has been shown that myristoylated proteins in cells regulate the signal transduction between membranes and cytoplasmic fractions. An algorithm we have developed to identify myristoylated proteins in cells predicts the presence of hundreds of myristoylated proteins. Interestingly, a large portion of the myristoylated proteins thought to take part in signal transduction between membranes and cytoplasmic fractions are included in the predicted myristoylated proteins. If the proteins functionally regulated by myristoylation, a posttranslational protein modification, were understood as cross-talk points within the intracellular signal transduction system, known signaling pathways could thus be linked to each other, and a novel map of this intracellular network could be constructed. On the basis of our recent results, this review will highlight the multifunctional aspects of protein N-myristoylation in brain.

Show MeSH
Related in: MedlinePlus