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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

The radius of gyration as a function of the molar ratio of mC/N9 to Ca2+/CaM at a CaM concentration of 9.0 mg/mL.
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fig06: The radius of gyration as a function of the molar ratio of mC/N9 to Ca2+/CaM at a CaM concentration of 9.0 mg/mL.

Mentions: SAXS can capture structural transformations of proteins in solution in terms of changes in the radius of gyration. The SAXS analysis indicated that the binding of two mC/N9 molecules induced a drastic structural change in Ca2+/CaM (Fig. 6). The radius of gyration for the Ca2+/CaM-mC/N9 complex was 19.8 ± 0.3 Å (Table 2). This value was significantly smaller than that of Ca2+/CaM (21.9 ± 0.3 Å), which adopted a dumbbell structure and was 2–3 Å larger than those of the complexes of Ca2+/CaM with the non-myristoylated target peptides of MLCK or CaM kinase II, which adopted a compact globular structure.36) The pair distance distribution function had no shoulder peak at around 40 Å which was mainly due to the dumbbell structure. These results suggested that Ca2+/CaM interacted with Nα-myristoylated CAP-23/NAP-22 differently than it did with other non-myristoylated target proteins.


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)

The radius of gyration as a function of the molar ratio of mC/N9 to Ca2+/CaM at a CaM concentration of 9.0 mg/mL.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

fig06: The radius of gyration as a function of the molar ratio of mC/N9 to Ca2+/CaM at a CaM concentration of 9.0 mg/mL.
Mentions: SAXS can capture structural transformations of proteins in solution in terms of changes in the radius of gyration. The SAXS analysis indicated that the binding of two mC/N9 molecules induced a drastic structural change in Ca2+/CaM (Fig. 6). The radius of gyration for the Ca2+/CaM-mC/N9 complex was 19.8 ± 0.3 Å (Table 2). This value was significantly smaller than that of Ca2+/CaM (21.9 ± 0.3 Å), which adopted a dumbbell structure and was 2–3 Å larger than those of the complexes of Ca2+/CaM with the non-myristoylated target peptides of MLCK or CaM kinase II, which adopted a compact globular structure.36) The pair distance distribution function had no shoulder peak at around 40 Å which was mainly due to the dumbbell structure. These results suggested that Ca2+/CaM interacted with Nα-myristoylated CAP-23/NAP-22 differently than it did with other non-myristoylated target proteins.

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