The Second Messenger Binding Site of Inositol 1,4,5-Trisphosphate 3-Kinase Is Centered in the Catalytic Domain and Related to the Inositol Trisphosphate Receptor Site

Bertsch, Uwe; Deschermeier, Christina; Fanick, Werner; Girkontaitė, Irutė; Hillemeier, Kirsten; Johnen, Heiko; Weglöhner, Wolfgang; Emmrich, Frank; Mayr, Georg W.

doi:10.1074/jbc.275.3.1557

Cited by 26 publications

(18 citation statements)

References 37 publications

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“…Amino acid residues showing similarity to a segment of the Ins(1,4,5)P $ receptor [35] were also seen in the sequence of Ins(1,4,5)P $ 3-kinase C (i.e. LVKARERPRPR&!().…”

Section: Identification Of a Potential Initiator Codonmentioning

confidence: 98%

Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C

Dewaste

Pouillon

Moreau

et al. 2000

Biochemical Journal

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Inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] 3-kinase catalyses the phosphorylation of Ins(1,4,5)P3 to Ins(1,3,4,5)P4. cDNAs encoding two isoenzymes of Ins(1,4,5)P3 3-kinase (3-kinases A and B) have been described previously. In the present study, we report the cloning of a full-length 2052bp cDNA encoding a third human isoenzyme of the Ins(1,4,5)P3 3-kinase family, referred to as isoform C. This novel enzyme has a calculated molecular mass of 75.207kDa and a Km for Ins(1,4,5)P3 of 6µM. Northern-blot analysis showed the presence of a transcript of approx. 3.9kb in various human tissues. Inositol trisphosphate 3-kinase C demonstrates enzymic activity when expressed in DH5αF′ bacteria or COS-7 cells. Calcium alone decreases the Ins(1,4,5)P3 3-kinase activity of the 3-kinase C isoenzyme in transfected COS-7 cells. This inhibitory effect is reversed in the presence of calmodulin. The recombinant bacterial 3-kinase C can be adsorbed on calmodulin–Sepharose in the presence of calcium. The present data show that Ins(1,4,5)P3 3-kinase C: (i) shares a conserved catalytic domain of about 275 amino acids with the two other mammalian isoforms, (ii) could be purified on a calmodulin–Sepharose column and (iii) could be distinguished from the A and B isoenzymes by the effects of calcium and of calmodulin.

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“…Amino acid residues showing similarity to a segment of the Ins(1,4,5)P $ receptor [35] were also seen in the sequence of Ins(1,4,5)P $ 3-kinase C (i.e. LVKARERPRPR&!().…”

Section: Identification Of a Potential Initiator Codonmentioning

confidence: 98%

Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C

Dewaste

Pouillon

Moreau

et al. 2000

Biochemical Journal

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“…In a tightly regulated manner, these second messengers may be recycled by further phosphorylation of Ins(1, 4, 5)P 3 to Ins(1, 3, 4, 5)P 4 by Ins (1, 4, 5) P 3 3-kinase (IP3K), or dephosphorylation to Ins(1, 4)P 2 by inositol polyphosphate 5-phosphatase (IPPase). To date, most molecular characterizations, expression pattern analyses and biochemical studies have focused on key PI pathway-related proteins including PIS [5], PI4K [6][7][8], PIP5K [9][10][11][12][13], PLC [14,15], PLD [16], PLA 1 [17], PLA 2 [18,19], PI 3-kinase (PI3K) [20], IPPase [21] and inositol 1, 3, 4-trisphosphate 5/6-kinase (IP 3 5/6K) [22]. In contrast, little attention has been paid to other proteins such as inositol 1, 4, 5-trisphosphate receptor (IP 3 R) and PI transfer protein (PITP), and there are many other signal molecules yet to be investigated within this pathway.…”

Section: Introductionmentioning

confidence: 99%

DNA chip-based expression profile analysis indicates involvement of the phosphatidylinositol signaling pathway in multiple plant responses to hormone and abiotic treatments

Lin

Rui

et al. 2004

Cell Res

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The phosphatidylinositol (PI) metabolic pathway is considered critical in plant responses to many environmental factors, and previous studies have indicated the involvement of multiple PI-related gene families during cellular responses. Through a detailed analysis of the Arabidopsis thaliana genome, 82 polypeptides were identified as being involved in PI signaling. These could be grouped into different families including PI synthases (PIS), PI-phosphate kinases (PIPK), phospholipases (PL), inositol polyphosphate phosphatases (IPPase), inositol polyphosphate kinases (IPK), PI transfer proteins and putative inositol polyphosphate receptors. The presence of more than 10 isoforms of PIPK, PLC, PLD and IPPase suggested that these genes might be differentially expressed during plant cellular responses or growth and development. Accordingly, DNA chip technology was employed to study the expression patterns of various isoforms. In total, 79 mRNA clones were amplified and used for DNA chip generation. Expression profile analysis was performed using samples that represented multiple tissues or cellular responses. Tested samples included normal leaf, stem and flower tissues, and leaves from plants treated with various hormones (auxin, cytokinin, gibberellin, abscisic acid and brassinosteroid) or environmental factors (temperature, calcium, sodium, drought, salicylic acid and jasmonic acid). Results showed that many PI pathway-related genes were differentially expressed under these experimental conditions. In particular, the different isoforms of each family were specifically expressed in many cases, suggesting their involvement in tissue specificity and cellular responses to environmental conditions. This work provides a starting point for functional studies of the relevant PI-related proteins and may help shed light onto the role of PI pathways in development and cellular responses.

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“…This consensus sequence, P-x-x-x-D-x-K-x-G, is required for the catalytic activity of InsP 3 kinase (InsP 3 K) (12). Recently, Mayr and associates (13) established that this domain modulates the catalytic site for phosphate transfer from ATP to the inositol ring. In a search for additional members of the inositol polyphosphate kinase family, we screened expressed sequence tag (EST) databases for proteins containing this consensus sequence.…”

mentioning

confidence: 99%

“…Total RNA from various rat organs was prepared using LiCl precipitation methods (17). RNA (10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20) g) was loaded on 1% agarose͞formaldehyde͞Mops gel and transferred to Hybond N ϩ nylon membrane (Amersham Pharmacia). ORFs for rat IPMK were labeled with [␣-32 P]dCTP using oligo labeling as described (17).…”

mentioning

confidence: 99%

Mammalian inositol polyphosphate multikinase synthesizes inositol 1,4,5-trisphosphate and an inositol pyrophosphate

Saiardi

Nagata

Luo

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

101

112

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The Second Messenger Binding Site of Inositol 1,4,5-Trisphosphate 3-Kinase Is Centered in the Catalytic Domain and Related to the Inositol Trisphosphate Receptor Site

Cited by 26 publications

References 37 publications

Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C

Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C

DNA chip-based expression profile analysis indicates involvement of the phosphatidylinositol signaling pathway in multiple plant responses to hormone and abiotic treatments

Mammalian inositol polyphosphate multikinase synthesizes inositol 1,4,5-trisphosphate and an inositol pyrophosphate

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