Myristoylation-regulated Direct Interaction Between Calcium-bound Calmodulin and N-terminal Region of pp60v-src

Hayashi, Nobuhiro; Nakagawa, Chisako; Ito, Yutaka; Takasaki, Akihiko; Jinbo, Yuji; Yamakawa, Yoshinori; Titani, Koiti; Hashimoto, Keiichiro; Izumi, Yoshinobu; Matsushima, Norio

doi:10.1016/j.jmb.2004.02.041

Cited by 22 publications

(22 citation statements)

References 38 publications

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“…In fact, it has been suggested that Src kinase may be regulated by the same mechanism found in the case of CAP-23/NAP-22. 46) To stably anchor src kinase on the membranes, certain coupling factors are likely to be needed in addition to myristoylation of the protein.…”

Section: Physiological Function Of Myristoylationmentioning

confidence: 99%

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

Hayashi

Titani

2010

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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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 Nα-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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Section: Physiological Function Of Myristoylationmentioning

confidence: 99%

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

Hayashi

Titani

2010

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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“…The capacity of CaM to bind directly to the N-terminal myristoyl group of other proteins has been tested for viral proteins such as Nef of HIV1 [86] and the pp60v-src tyrosine protein kinase [87]. These proteins posses an N-terminal group followed by a cluster of basic residues similar to mNAP.…”

Section: Cortical Cytoskeleton-associated Pro-tein/neuron-specific Acmentioning

confidence: 99%

Protein-Peptide Interaction Studies Demonstrate the Versatility of Calmodulin Target Protein Binding

Ishida¹,

Vogel

2006

PPL

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Calmodulin (CaM) is a prototypical Ca2+-sensor protein that can control many important biological functions by binding to hundreds of target proteins. To gain insight into the versatility of CaM-target recognition, we have analyzed the complex structures for many types of CaM-binding peptides and some target proteins. In particular, some recently reported novel complex structures reveal that the versatile target binding of CaM is accommodated by its flexible domain arrangement and the malleability of its interfaces.

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“…All of the NMR spectra were measured at 310 K on a Bruker DMX-500 spectrometer (Hayashi et al, 2004). TFP was titrated in aliquots of 0.33 protein equivalents into a uniformly 13 C/ 15 N-labelled sample of the protein.…”

Section: Nuclear Magnetic Resonancementioning

confidence: 99%

Binding of trifluoperazine to apocalmodulin revealed by a combination of small-angle X-ray scattering and nuclear magnetic resonance

et al. 2007

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Small-angle X-ray scattering (SAXS) and nuclear magnetic resonance (NMR) studies were performed to investigate the binding of trifluoperazine (TFP) to Ca 2+ -free calmodulin (apoCaM) with N-and C-terminal globular domains connected by a linker. The SAXS and NMR measurements were taken throughout the titration of TFP. The SAXS analyses indicate that the binding of TFP induces structural changes from a dumbbell shape to a compact globular shape in solution. The formation of the complete globular structure requires 5.0 added equivalents of TFP. An analysis of NMR chemical-shift changes indicates that the C-terminal domain of apoCaM is involved in the binding of TFP. The SAXS and NMR data reflect the high structural flexibility of apoCaM.

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Myristoylation-regulated Direct Interaction Between Calcium-bound Calmodulin and N-terminal Region of pp60v-src

Cited by 22 publications

References 38 publications

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

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

Protein-Peptide Interaction Studies Demonstrate the Versatility of Calmodulin Target Protein Binding

Binding of trifluoperazine to apocalmodulin revealed by a combination of small-angle X-ray scattering and nuclear magnetic resonance

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