Structure of the Neuronal Protein Calexcitin Suggests a Mode of Interaction in Signalling Pathways of Learning and Memory

Erskine, P.T.; Beaven, G. D. E.; Hagan, Robert M.; Findlow, I.S.; Werner, Jörn M.; Wood, Steve; Vernon, Jeffrey; Giese, K. Peter; Fox, Gavin C.; Cooper, J.B.

doi:10.1016/j.jmb.2006.01.083

Cited by 14 publications

(8 citation statements)

References 36 publications

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“…Another up-regulated protein in forager brain was identified as similar to the gene of Drosophila melanogaster sarcoplasmic calcium-binding protein 2 (dSCP2), whose product gave juvenile hormone diol kinase (JDHK) activity and showed high similarity to JHDK from Manduca sexta . Molecular modeling and crystal three-dimensional structure of these proteins revealed structural similarity to G-proteins and calcium binding proteins. , Proteomics and in situ hybridization analysis revealed that JHDK expression was up-regulated in MBs of forager honey bee brains . JHDK is an important enzyme involved in the juvenile hormone (JH) inactivation pathway.…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Honey Bee Brain upon Ontogenetic and Behavioral Development

et al. 2009

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The honey bee (Apis mellifera) is a social insect that shows complex and integrated behaviors. Its ability to read and respond to several sets of extrinsic and intrinsic signals is fundamental for the modulation of individual activities and social systems. For instance, A. mellifera behavior changes upon the ontogenetic differentiation from nurse to forager worker subcastes. In this work, brain proteomes of nurses and foragers were compared by two-dimensional gel electrophoresis within pH range of 4-7 in order to find proteins related to such an ontogenetic and behavioral development. Twenty differentially expressed proteins were detected by gel image computational analysis, and identified by peptide mass fingerprinting using MALDI-TOF mass spectrometry. Nurse brain showed increased expression of major royal jelly proteins (MRJP1, MRJP2 and MRJP7), which are related to determination of castes during the honey bee larvae differentiation. Immunocytochemistry and electron microscopy showed that MRJP1 was localized in the cytoplasm of brain cells, seemingly along filaments of the cytoskeleton, in the antennal lobe, optical lobe and mushroom body. Also, MRJP1 was deposited on the rhabdom, a structure of the retinular cells, composed of numerous tubules. Such evidence suggests that MRJP1 could be associated to proteins of filamentous structures. MRJP1 was also found in intercellular spaces between cells in mushrooms bodies, indicating that it is a secreted protein. Other proteins implicated in protein synthesis and putative functions in the olfactory system were also up-regulated in the nurse brain. Experienced foragers overexpressed proteins possibly involved in energy production, iron binding, metabolic signaling and neurotransmitter metabolism. Such differential expression of proteins may be related to ontogenetic and behavior changes in A. mellifera.

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Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Honey Bee Brain upon Ontogenetic and Behavioral Development

et al. 2009

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“…They include the photoproteinb erovin from ac omb jelly, [18] the nonluminescent coelenterazineb inding protein (CBP) from as ea pansy, [19] the GTPase calexcitin from as ea squid, [20] and two sarcoplasmic calcium binding proteins (SCBPs) from earthworms. They include the photoproteinb erovin from ac omb jelly, [18] the nonluminescent coelenterazineb inding protein (CBP) from as ea pansy, [19] the GTPase calexcitin from as ea squid, [20] and two sarcoplasmic calcium binding proteins (SCBPs) from earthworms.…”

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confidence: 99%

“…OABP2.1 also shares structural similarity with several calcium binding proteins, mainly from marine invertebrates. They include the photoproteinb erovin from ac omb jelly, [18] the nonluminescent coelenterazineb inding protein (CBP) from as ea pansy, [19] the GTPase calexcitin from as ea squid, [20] and two sarcoplasmic calcium binding proteins (SCBPs) from earthworms. [21,22] Although the sequence homologies are low,t hey all share similaro verall conformations ( Figure 4A).…”

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confidence: 99%

Crystal Structure of Okadaic Acid Binding Protein 2.1: A Sponge Protein Implicated in Cytotoxin Accumulation

et al. 2015

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Okadaic acid (OA) is a marine polyether cytotoxin that was first isolated from the marine sponge Halichondria okadai. OA is a potent inhibitor of protein serine/threonine phosphatases (PP) 1 and 2A, and the structural basis of phosphatase inhibition has been well investigated. However, the role and mechanism of OA retention in the marine sponge have remained elusive. We have solved the crystal structure of okadaic acid binding protein 2.1 (OABP2.1) isolated from H. okadai; it has strong affinity for OA and limited sequence homology to other proteins. The structure revealed that OABP2.1 consists of two α-helical domains, with the OA molecule deeply buried inside the protein. In addition, the global fold of OABP2.1 was unexpectedly similar to that of aequorin, a jellyfish photoprotein. The presence of structural homologues suggested that, by using similar protein scaffolds, marine invertebrates have developed diverse survival systems adapted to their living environments.

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“…Its elevated expression was observed during neuronal differentiation and migration [Fairless et al, 2019]. Similarly, calexcitin interacts with voltage-dependent potassium channel proteins and controls neuronal firing [Erskine et al, 2006]. Binding of Ca 2+ to EF-hand in calmodulin triggers its Ca 2+ sensor activity by inducing conformational changes, which in turn exposes its hydrophobic targetbinding surface [Halling et al, 2016].…”

Section: Importance Of Ca 2+mentioning

confidence: 99%

The Role of Calcium Signaling in Regulation of Epithelial-Mesenchymal Transition

Adiga

Radhakrishnan

Chakrabarty

et al. 2020

Cells Tissues Organs

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Despite substantial advances in the field of cancer therapeutics, metastasis is a significant challenge for a favorable clinical outcome. Epithelial to mesenchymal transition (EMT) is a process of acquiring increased motility, invasiveness, and therapeutic resistance by cancer cells for their sustained growth and survival. A plethora of intrinsic mechanisms and extrinsic microenvironmental factors drive the process of cancer metastasis. Calcium (Ca2+) signaling plays a critical role in dictating the adaptive metastatic cell behavior comprising of cell migration, invasion, angiogenesis, and intravasation. By modulating EMT, Ca2+ signaling can regulate the complexity and dynamics of events leading to metastasis. This review summarizes the role of Ca2+ signal remodeling in the regulation of EMT and metastasis in cancer.

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Structure of the Neuronal Protein Calexcitin Suggests a Mode of Interaction in Signalling Pathways of Learning and Memory

Cited by 14 publications

References 36 publications

Proteomic Analysis of Honey Bee Brain upon Ontogenetic and Behavioral Development

Proteomic Analysis of Honey Bee Brain upon Ontogenetic and Behavioral Development

Crystal Structure of Okadaic Acid Binding Protein 2.1: A Sponge Protein Implicated in Cytotoxin Accumulation

The Role of Calcium Signaling in Regulation of Epithelial-Mesenchymal Transition

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