Regulation of the Dual Specificity Protein Phosphatase, DsPTP1, through Interactions with Calmodulin

Yoo, Jae Hyuk; Cheong, Mi Sun; Park, Chan Young; Moon, Byeong Cheol; Kim, Min Chul; Kang, Yun Hwan; Park, Hyeong Cheol; Choi, Man Soo; Lee, Ju Huck; Jung, Won Yong; Yoon, Hae Won; Chung, Woo Sik; Lim, Chae Oh; Lee, Sang Yeol; Cho, Moo Je

doi:10.1074/jbc.m310709200

Cited by 34 publications

(32 citation statements)

References 71 publications

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“…13,14,23 In this study, we screened an Arabidopsis cDNA expression library constructed from heat-treated plant seedlings using AtCaM2::HRP as a probe. 20,22 In all, 11 positive clones were obtained from a total of 5 Â 10 5 recombinant phages. Based on the restriction patterns of plasmid inserts, the genes coding for CaMBPs were classified into seven different loci.…”

Section: Resultsmentioning

confidence: 99%

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AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants

et al. 2005

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Calmodulin (CaM) influences many cellular processes by interacting with various proteins. Here, we isolated AtBAG6, an Arabidopsis CaM-binding protein that contains a central BCL-2-associated athanogene (BAG) domain. In yeast and plants, overexpression of AtBAG6 induced cell death phenotypes consistent with programmed cell death (PCD). Recombinant AtBAG6 had higher affinity for CaM in the absence of free Ca 2 þ than in its presence. An IQ motif (IQXXXRGXXXR, where X denotes any amino-acid) was required for Ca 2 þ -independent CaM complex formation and single amino-acid changes within this motif abrogated both AtBAG6-activated CaM-binding and cell death in yeast and plants. A 134-amino-acid stretch, encompassing both the IQ motif and BAG domain, was sufficient to induce cell death. Agents generating oxygen radicals, which are known to be involved in plant PCD, specifically induced the AtBAG6 transcript. Collectively, these results suggest that AtBAG6 is a stress-upregulated CaM-binding protein involved in plant PCD.

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Section: Resultsmentioning

confidence: 99%

“…[20][21][22] Here, we report the isolation and characterization of an Arabidopsis gene encoding a BAG protein homolog (AtBAG6). Our data indicate that AtBAG6 expression in yeast and plant cells induces cell death.…”

Section: Introductionmentioning

confidence: 99%

AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants

et al. 2005

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“…It has recently been demonstrated that NtMKP1 can be activated by its substrate SIPK but not by Ca 2ϩ -CaM; as such, the role of the Ca 2ϩ -CaM binding to NtMKP1 is less obvious (51). It is possible that it might involve a substrate-specific regulation by Ca 2ϩ -CaM similar to another plant phosphatase, DsPTP1 (52). On the other hand, the role of Ca 2ϩ -CaM binding is not always limited to enzyme activation.…”

Section: Camentioning

confidence: 97%

Structural Studies of Soybean Calmodulin Isoform 4 Bound to the Calmodulin-binding Domain of Tobacco Mitogen-activated Protein Kinase Phosphatase-1 Provide Insights into a Sequential Target Binding Mode

Ishida

Rainaldi

Vogel

2009

Journal of Biological Chemistry

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The calcium regulatory protein calmodulin (CaM) binds in a calcium-dependent manner to numerous target proteins. The calmodulin-binding domain (CaMBD) region of Nicotiana tabacum MAPK phosphatase has an amino acid sequence that does not resemble the CaMBD of any other known Ca 2؉ -CaMbinding proteins. Using a unique fusion protein strategy, we have been able to obtain a high resolution solution structure of the complex of soybean Ca 2؉ -CaM4 (SCaM4) and this CaMBD. Complete isotope labeling of both parts of the complex in the fusion protein greatly facilitated the structure determination by NMR. The 12-residue CaMBD region was found to bind exclusively to the C-lobe of SCaM4. A specific Trp and Leu side chain are utilized to facilitate strong binding through a novel ''double anchor'' motif. Moreover, the orientation of the helical peptide on the surface of Ca 2؉ -SCaM4 is distinct from other known complexes. The N-lobe of Ca 2؉ -SCaM4 in the complex remains free for additional interactions and could possibly act as a calcium-dependent adapter protein.Signaling through the MAPK pathway and increases in intracellular Ca 2؉ are both hallmarks of the plant stress response, and our data support the notion that coordination of these responses may occur through the formation of a unique CaM-MAPK phosphatase multiprotein complex. Calmodulin (CaM)2 is a ubiquitous intracellular Ca 2ϩ sensor protein that plays an essential role in various Ca 2ϩ signaling pathways. Contiguous and unique CaM-binding domain (CaMBD) regions are found widely distributed in many different types of CaM target proteins including protein phosphatases and kinases, cytoskeletal proteins, ion channels, and pumps (1, 2). Even though the CaMBD from various proteins share relatively poor amino acid sequence similarity, the majority of CaMBD become ␣-helical upon binding to CaM, and they can be grouped into either the 1-5-10 or the 1-8-14 motif, where the first and the last number indicate the position of two hydrophobic anchor residues that attach the CaMBD to the two binding pockets of the bilobal Ca 2ϩ -CaM. However, several noncanonical classes of CaMBD have also been identified. For example, in the CaMBD of the MARCKS protein, the two anchor residues are separated by a single amino acid residue (3). On the other hand, in the recently determined crystal structure of Ca 2ϩ -CaM complexed with the CaMBD of the skeletal muscle ryanodine receptor RYR1, they are separated by 15 residues (1-17 motif) (4). Bulky hydrophobic side chains of residues such as Trp, Leu, Phe, and Ile are most commonly utilized as anchor residues (see Fig. 1a), and these are usually deeply inserted into the hydrophobic target-binding pocket of either the N-or C-lobe of Ca 2ϩ -CaM. However, in several cases, including the N-methyl-D-aspartate receptors (NMDAR) (5) and the voltage-gated Ca 2ϩ channels (Cav1-2) (6, 7), a polar side chain from Thr or Tyr has also been found to act as an anchor residue. In almost all Ca 2ϩ -CaM complexes studied to date, the two lobes of Ca 2ϩ -CaM bec...

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“…To examine the CaM-binding ability of recombinant proteins, a duplicate blot was probed with AtCaM2::HRP conjugate in the presence of 1 mM CaCl 2 or 5 mM EGTA. The CaM:HRP overlay assay was carried out as described previously (29). Bound CaM was visualized using an ECL detection system (Amersham Biosciences).…”

Section: Methodsmentioning

confidence: 99%

“…Screening of Arabidopsis cDNA Expression Library-Screening of the Arabidopsis cDNA expression library using HRPconjugated AtCaM2 (AtCaM2::HRP) was carried out as described in previous reports (28,29).…”

Section: Methodsmentioning

confidence: 99%

Identification of a Calmodulin-binding NAC Protein as a Transcriptional Repressor in Arabidopsis

Kim

Park²,

Yoo

et al. 2007

Journal of Biological Chemistry

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Regulation of the Dual Specificity Protein Phosphatase, DsPTP1, through Interactions with Calmodulin

Cited by 34 publications

References 71 publications

AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants

AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants

Structural Studies of Soybean Calmodulin Isoform 4 Bound to the Calmodulin-binding Domain of Tobacco Mitogen-activated Protein Kinase Phosphatase-1 Provide Insights into a Sequential Target Binding Mode

Identification of a Calmodulin-binding NAC Protein as a Transcriptional Repressor in Arabidopsis

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