Novel frequenin-modulated Ca2+-signaling membrane guanylate cyclase (ROS-GC) transduction pathway in bovine hippocampus

Fik-Rymarkiewicz, Ewa; Duda, Teresa; Sharma, Rameshwar K.

doi:10.1007/s11010-006-9215-6

Cited by 18 publications

(27 citation statements)

References 55 publications

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“…For PIP 2 , and many other molecules, one would like to use Ca as a model for local signaling, and local linkages between local Ca signals and PIP 2 signaling are very attractive. For example, both phosphatidylinositol (PI)-4 kinases [24,27,30] and phosphatidylinositol-phosphate (PIP)-5 kinases [3,4,67], as well as phospholipase C's [81], are activated by cytoplasmic Ca in different cells. One would like to imagine that PIP 2 metabolism can respond to and interact with Ca in a local fashion, especially as Ca signals amplify and propagate via Ca-dependent release of Ca from internal stores [14,42,44,71].…”

Section: Introductionmentioning

confidence: 99%

Local PIP2 signals: when, where, and how?

Hilgemann

2007

Pflugers Arch - Eur J Physiol

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PIP(2) is a minor phospholipid that modulates multiple cellular processes. However, its abundance by mass, like diacylglycerol, is still 20 to 100 times greater than the master phospholipid second messenger, PIP(3). Therefore, it is a case-by-case question whether PIP(2) is acting more like GTP, in being a cofactor in regulatory processes, or whether it is being used as a true second messenger. Analysis of signaling mechanisms in primary cells is essential to answer this question, as overexpression studies will naturally generate false positives. In connection with the possible messenger function of PIP(2), a second question arises as to how and if PIP(2) metabolism and signaling may be limited in space. This review summarizes succinctly the notable cases in which PIP(2) is proposed to function in a localized way and the different mechanistic models that may allow it to function locally. In general, drastic restrictions of PIP(2) diffusion are required. It is speculated that molecular PIP(2) signaling may be possible in the absence of PIP(2) gradients via ternary complexes between PIP(2) and two protein partners. That PIP(2) synthesis and hydrolysis might be locally dependent on protein-protein interactions, and direct lipid "hand-off" is suggested by multiple results.

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Section: Introductionmentioning

confidence: 99%

Local PIP2 signals: when, where, and how?

Hilgemann

2007

Pflugers Arch - Eur J Physiol

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“…All the above proteins also modulate the GUCY2F product (ROS-GC2/ RetGC2) in a similar fashion, albeit at differing efficiencies as assessed by fold-change in activity and EC 50 values [39,51]. Frequenin [44] and HPCA [45] activate the olfactory guanylate cyclase (ONE-GC/GC-D) at elevated calcium concentrations; interestingly, so does GCAP1 [41]. VSNL1, on the other hand, activates the product of NPR2B (atrial natriuretic peptide receptor type B/GC-B) [26,42,43].…”

Section: Intricacy Of Ncs/mgc Interactionsmentioning

confidence: 99%

“…modulate mGC activity [26,27,[42][43][44][45][46]. However, in addition to mGC, each member of the VILIP group is known to interact with multiple targets, generating perhaps the most functionally diverse group among the three [21, 22,25].…”

Section: Tissue Expression Analysismentioning

confidence: 99%

“…It has now been demonstrated that all KChIPs share DNA-binding ability also [48]. Interestingly, between the two outgrouped members, frequenin activates mGC [44] but recoverin does not; instead, it regulates rhodopsin kinase [49] and contributes to the feedback loop in phototransduction [50,51]. Thus, members of the GCAP and VILIP groups as well as the outgrouped frequenin share the ability to modulate mGC activity.…”

Section: Tissue Expression Analysismentioning

confidence: 99%

“…A57 is highly conserved in GCAPs as well as most VILIPs but is replaced by a Pro residue in recoverin and frequenin. Neither of these proteins interacts with ROS-GC1 ( [44]; reviewed in: [49]). Therefore, could this residue be critical for ROS-GC1 interaction?…”

Section: Gcap2 Modulation Of Ros-gc1mentioning

confidence: 99%

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Evolutionary Interrelationships and Insights into Molecular Mechanisms of Functional Divergence: An Analysis of Neuronal Calcium Sensor Proteins

Viviano¹,

Wu²,

Venkataraman³

2013

J Phylogen Evolution Biol

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The normal function of any organism, its organizational complexity notwithstanding, depends on the interaction of its proteins with their targets. Thus, analysis of target site interaction is an essential part of all biology. At the protein level, such analyses are critical to both mechanistic knowledge and potential clinical applications such as drug discovery. Approaches to map amino acid residues involved in target site interaction typically are experimental or are based on three-dimensional structures obtained through crystallography. Here we test a novel approach that combines phylogenetic analyses with mining of experimental data using neuronal calcium sensor proteins. The proteins fall into three groups based on sequence comparison. One interaction was taken up for analysis from each group. Using the sequence divergence to evaluate the role of amino acids identified experimentally to form the interface with the target, we demonstrate that it is possible to predict residues that are likely to contribute to the specificity of the interaction and, therefore, the functional divergence. Thus, evolutionary analyses of proteins provide an important addition in approaches to generate refined maps of target site interactions in proteins. This approach is especially useful in delineating the functional divergence in a family of closely related proteins.

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Hippocalcin, new Ca2+ sensor of a ROS-GC subfamily member, ONE-GC, membrane guanylate cyclase transduction system

et al. 2009

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Hippocalcin is a member of the neuronal Ca 2+ sensor protein family. Among its many biochemical functions, its established physiological function is that via neuronal apoptosis inhibitory protein it protects the neurons from Ca 2+ -induced cell death. The precise biochemical mechanism/s through which hippocalcin functions, is not clear. In the present study, a new mechanism by which it functions is defined. The bovine form of hippocalcin (BovHpca) native to the hippocampus has been purified, sequenced, cloned and studied. The findings show that there is the evolutionary conservation of its structure. It is a Ca 2+ -sensor of a variant form of the ROS-GC subfamily of membrane guanylate cyclases, ONE-GC. It senses physiological increments of Ca 2+ with a K 1/2 of 0.5 μM and stimulates ONE-GC or ONE-GC-like membrane guanylate cyclase. The Hpca-modulated ONE-GC-like transduction system exists in the hippocampal neurons. And hippocalcin-modulated ONE-GC transduction system exists in the olfactory receptor neuroepithelium. The Hpca-gene knock out studies demonstrate that the portion of this is about 30% of the total membrane guanylate cyclase transduction system. The findings establish Hpca as a new Ca 2+ sensor modulator of the ROS-GC membrane guanylate cyclase transduction subfamily. They support the concept on universality of the presence and operation of the ROS-GC transduction system in the sensory and sensory-linked neurons. They validate that the ROS-GC transduction system exists in multiple forms. And they provide an additional mechanism by which ROS-GC subfamily acts as a transducer of the Ca 2+ signals originating in the neurons.

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Novel frequenin-modulated Ca2+-signaling membrane guanylate cyclase (ROS-GC) transduction pathway in bovine hippocampus

Cited by 18 publications

References 55 publications

Local PIP2 signals: when, where, and how?

Local PIP2 signals: when, where, and how?

Evolutionary Interrelationships and Insights into Molecular Mechanisms of Functional Divergence: An Analysis of Neuronal Calcium Sensor Proteins

Hippocalcin, new Ca2+ sensor of a ROS-GC subfamily member, ONE-GC, membrane guanylate cyclase transduction system

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