Inositol 1,4,5‐trisphosphate receptor (type 1) phosphorylation and modulation by Cdc2

Malathi, Krishnamurthy; Kohyama, Shinya; Ho, Michael; Soghoian, Damien Z.; Li, Xiaogui; Silane, Michael; Berenstein, Alejandro; Jayaraman, Thottala

doi:10.1002/jcb.10720

Cited by 47 publications

(65 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In a previous study, we reported that a cell cycle-dependent kinase, cdc2, phosphorylates IP 3 R1 in vitro and in vivo (3). This observation is consistent with previous reports that IP 3 -gated calcium release is modulated during the cell cycle (18 -20).…”

supporting

confidence: 92%

“…T he inositol 1,4,5-trisphosphate (IP 3 ) 4 -gated intracellular Ca 2ϩ release, resulting from the activation of receptor tyrosine kinases and G protein-coupled receptors, is an important regulator of various cellular processes, including proliferation and apoptosis (1)(2)(3)(4)(5)(6)(7). Several endogenous and exogenous activators of IP 3 R1 have been reported, including phosphorylation, positive and negative feedback by Ca 2ϩ , and association with other accessory molecules (3, 8 -17).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Cdc2/Cyclin B1 Interacts with and Modulates Inositol 1,4,5-Trisphosphate Receptor (Type 1) Functions

Malathi

Križanová

et al. 2005

The Journal of Immunology

Self Cite

View full text Add to dashboard Cite

The resistance of inositol 1,4,5-trisphosphate receptor (IP3R)-deficient cells to multiple forms of apoptosis demonstrates the importance of IP3-gated calcium (Ca2+) release to cellular apoptosis. However, the specific upstream biochemical events leading to IP3-gated Ca2+ release during apoptosis induction are not known. We have shown previously that the cyclin-dependent kinase 1/cyclin B (cdk1/CyB or cdc2/CyB) complex phosphorylates IP3R1 in vitro and in vivo at Ser421 and Thr799. In this study, we show that: 1) the cdc2/CyB complex directly interacts with IP3R1 through Arg391, Arg441, and Arg871; 2) IP3R1 phosphorylation at Thr799 by the cdc2/CyB complex increases IP3 binding; and 3) cdc2/CyB phosphorylation increases IP3-gated Ca2+ release. Taken together, these results demonstrate that cdc2/CyB phosphorylation positively regulates IP3-gated Ca2+ signaling. In addition, identification of a CyB docking site(s) on IP3R1 demonstrates, for the first time, a direct interaction between a cell cycle component and an intracellular calcium release channel. Blocking this phosphorylation event with a specific peptide inhibitor(s) may constitute a new therapy for the treatment of several human immune disorders.

show abstract

supporting

confidence: 92%

mentioning

confidence: 99%

Cdc2/Cyclin B1 Interacts with and Modulates Inositol 1,4,5-Trisphosphate Receptor (Type 1) Functions

Malathi

Križanová

et al. 2005

The Journal of Immunology

Self Cite

View full text Add to dashboard Cite

show abstract

“…This conclusion is supported by mathematical modeling studies showing that increasing IP 3 R affinity is sufficient to replicate the behavior of elementary Ca 2þ release in eggs (Ullah et al, 2007). Furthermore, the affinity of the IP 3 R increases during mitosis apparently due to direct phosphorylation by MPF (Malathi et al, 2003(Malathi et al, , 2005. In contrast, in starfish eggs although the increase in Ca 2þ release was dependent on MPF activation, MPF does not directly phosphorylate the IP 3 R but rather mediates its effect through the actin cytoskeleton Santella et al, 2003).…”

Section: Physiological Roles Of Ca 2r At Fertilizationmentioning

confidence: 87%

Ca²⁺ signaling differentiation during oocyte maturation

Machaca

2007

Journal Cellular Physiology

View full text Add to dashboard Cite

Oocyte maturation is an essential cellular differentiation pathway that prepares the egg for activation at fertilization leading to the initiation of embryogenesis. An integral attribute of oocyte maturation is the remodeling of Ca 2þ signaling pathways endowing the egg with the capacity to produce a specialized Ca 2þ transient at fertilization that is necessary and sufficient for egg activation. Consequently, mechanistic elucidation of Ca 2þ signaling differentiation during oocyte maturation is fundamental to our understanding of egg activation, and offers a glimpse into Ca 2þ signaling regulation during the cell cycle.

show abstract

“…This study did not examine the role of this phosphorylation in eggs, although in microsome preparations MAPK IP 3 R1 phosphorylation decreased IP 3 binding and Ca 2þ release (Bai et al 2006). In contrast to this, phosphorylation of IP 3 R1 in somatic cells by Cdk1, which was observed to occur in several conserved Cdk1 motifs under in vitro and in vivo conditions, enhanced IP 3 binding and Ca 2þ release (Malathi et al 2003;Malathi et al 2005). IP 3 R1 phosphorylation within Cdk1 and MAPK consensus sites was reported in Xenopus oocytes and independent activation of these kinases increased IP 3 R-mediated Ca 2þ release ).…”

Section: Ip 3 R1 In MII Eggsmentioning

confidence: 89%

“…2). Following egg activation, it becomes gradually dephosphorylated and phosphorylation is not regained at first mitosis (Lee et al 2006 (Malathi et al 2003;Malathi et al 2005). IP 3 R1 phosphorylation within Cdk1 and MAPK consensus sites was reported in Xenopus oocytes and independent activation of these kinases increased IP 3 R-mediated Ca 2þ release ).…”

mentioning

confidence: 99%

Ca2+ Signaling During Mammalian Fertilization: Requirements, Players, and Adaptations

Wakai¹,

Vanderheyden²,

Fissore³

2011

Cold Spring Harbor Perspectives in Biology

View full text Add to dashboard Cite

Changes in the intracellular concentration of calcium ([Ca 2þ ] i ) represent a vital signaling mechanism enabling communication among cells and between cells and the environment. The initiation of embryo development depends on a [Ca 2þ ] i increase(s) in the egg, which is generally induced during fertilization. The [Ca 2þ ] i increase signals egg activation, which is the first stage in embryo development, and that consist of biochemical and structural changes that transform eggs into zygotes. The spatiotemporal patterns of [Ca 2þ ] i at fertilization show variability, most likely reflecting adaptations to fertilizing conditions and to the duration of embryonic cell cycles. In mammals, the focus of this review, the fertilization [Ca 2þ ] i signal displays unique properties in that it is initiated after gamete fusion by release of a sperm-derived factor and by periodic and extended [Ca 2þ ] i responses. Here, we will discuss the events of egg activation regulated by increases in [Ca 2þ ] i , the possible downstream targets that effect these egg activation events, and the property and identity of molecules both in sperm and eggs that underpin the initiation and persistence of the [Ca 2þ ] i responses in these species.A n increase in the intracellular concentration of calcium ([Ca 2þ ] i ) underlies the initiation, progression and/or completion of a wide variety of cellular processes, including fertilization, muscle contraction, secretion, cell division, and apoptosis (Berridge et al. 2000). To survive and proliferate, cells and organisms must communicate, and changes in [Ca 2þ ] i allow them to quickly respond to environmental, nutritional, or ligand challenges with responses that regulate cell fate and function. Cells devote significant amounts of their energy reserves to create and maintain ionic gradients between extracellular and intracellular milieus and also within the latter, thereby allowing brief alterations in these gradients to have profound signaling effects. In the case of Ca 2þ , myriad proteins have acquired the ability to bind Ca 2þ , which allows them to interpret and transform these elevations into cellular functions. This review will examine the cellular modifications induced by [Ca 2þ ] i changes during fertilization in mature mammalian oocytes, henceforth referred to as eggs.Oocytes during maturation ready themselves for fertilization and the initiation of embryogenesis. During this transition, oocytes undergo changes that include the resumption and progression of meiosis, the development of polyspermy-preventing mechanisms, the reorganization of the cytoskeleton with spindle formation and displacement to the cortex, and the translation, accumulation, and degradation of specific mRNAs and proteins involved in development (Horner and Wolfner 2008b (Stricker 1999;Miyazaki and Ito 2006). Elucidation of the signaling cascades and identification of the molecules/receptor(s) that initiate the Ca 2þ signal at fertilization has proven elusive, and this review will not dwell on th...

show abstract

Inositol 1,4,5‐trisphosphate receptor (type 1) phosphorylation and modulation by Cdc2

Cited by 47 publications

References 56 publications

Cdc2/Cyclin B1 Interacts with and Modulates Inositol 1,4,5-Trisphosphate Receptor (Type 1) Functions

Cdc2/Cyclin B1 Interacts with and Modulates Inositol 1,4,5-Trisphosphate Receptor (Type 1) Functions

Ca²⁺ signaling differentiation during oocyte maturation

Ca2+ Signaling During Mammalian Fertilization: Requirements, Players, and Adaptations

Contact Info

Product

Resources

About

Inositol 1,4,5‐trisphosphate receptor (type 1) phosphorylation and modulation by Cdc2

Cited by 47 publications

References 56 publications

Cdc2/Cyclin B1 Interacts with and Modulates Inositol 1,4,5-Trisphosphate Receptor (Type 1) Functions

Cdc2/Cyclin B1 Interacts with and Modulates Inositol 1,4,5-Trisphosphate Receptor (Type 1) Functions

Ca2+ signaling differentiation during oocyte maturation

Ca2+ Signaling During Mammalian Fertilization: Requirements, Players, and Adaptations

Contact Info

Product

Resources

About

Ca²⁺ signaling differentiation during oocyte maturation