Calmodulin-binding proteins: A journey of 40 years

Sharma, Rajendra K.; Parameswaran, Sreejit

doi:10.1016/j.ceca.2018.09.002

Cited by 50 publications

(42 citation statements)

References 96 publications

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“…Calmodulin (CaM) is a small protein that binds calcium ions via four EF-hand motifs [1]. Calcium-bound calmodulin undergoes conformational changes, forming a complex with increased affinity for many CaM-binding proteins [1][2][3]. Experiments demonstrate that calmodulin binds to a broad range of enzymatic and non-enzymatic proteins [4].…”

Section: Introductionmentioning

confidence: 99%

In Depth Analysis of Kinase Cross Screening Data to Identify CAMKK2 Inhibitory Scaffolds

et al. 2020

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The calcium/calmodulin-dependent protein kinase kinase 2 (CAMKK2) activates CAMK1, CAMK4, AMPK, and AKT, leading to numerous physiological responses. The deregulation of CAMKK2 is linked to several diseases, suggesting the utility of CAMKK2 inhibitors for oncological, metabolic and inflammatory indications. In this work, we demonstrate that STO-609, frequently described as a selective inhibitor for CAMKK2, potently inhibits a significant number of other kinases. Through an analysis of literature and public databases, we have identified other potent CAMKK2 inhibitors and verified their activities in differential scanning fluorimetry and enzyme inhibition assays. These inhibitors are potential starting points for the development of selective CAMKK2 inhibitors and will lead to tools that delineate the roles of this kinase in disease biology.

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Section: Introductionmentioning

confidence: 99%

In Depth Analysis of Kinase Cross Screening Data to Identify CAMKK2 Inhibitory Scaffolds

et al. 2020

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“…CaM has been documented to interact with hundreds of proteins, which in turn modifies a wide range of cellular processes [2,30,37]. As expected, with so many CaM interactions and functions, any alterations in CaM has potential implications for nearly every cell in the body.…”

Section: An Overwhelming Number Of Cam Interactionsmentioning

confidence: 83%

“…With notable roles in protein phosphorylation and dephosphorylation, cellular Ca 2+ metabolism, cyclic nucleotide metabolism, gene expression, cell proliferation, muscle contraction, and proteolysis, CaM modification and regulation has implications for nearly every cell in the body [2]. For a detailed discussion regarding the history of CaM discovery and the extensive number of interacting proteins and posited regulatory functions, we refer the reader to Sharma et al 2018 [2]. For a focused review on the roles of CaM in a cardiomyocyte, see Sorensen et al 2013 [3].…”

Section: Introductionmentioning

confidence: 99%

Calmodulin Mutations Associated with Heart Arrhythmia: A Status Report

Chazin

Johnson

2020

IJMS

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Calmodulin (CaM) is a ubiquitous intracellular Ca2+ sensing protein that modifies gating of numerous ion channels. CaM has an extraordinarily high level of evolutionary conservation, which led to the fundamental assumption that mutation would be lethal. However, in 2012, complete exome sequencing of infants suffering from recurrent cardiac arrest revealed de novo mutations in the three human CALM genes. The correlation between mutations and pathophysiology suggests defects in CaM-dependent ion channel functions. Here, we review the current state of the field for all reported CaM mutations associated with cardiac arrhythmias, including knowledge of their biochemical and structural characteristics, and progress towards understanding how these mutations affect cardiac ion channel function.

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“…Calmodulin is a protein activator that binds to many different proteins in a calcium-dependent and reversible manner [45]. Among the calmodulin-binding proteins, calcineurin has been found to be involved in apoptosis-related pathway initiation.…”

Section: Regulated Cell Death Of the Echinococcus Parasitementioning

confidence: 99%

Interactions between hydatid cyst and regulated cell death may provide new therapeutic opportunities

2019

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Cystic echinococcosis and alveolar echinococcosis are chronic zoonotic infections, transmitted throughout the world. Development of the cestode larval stages in the liver and lungs causes damage to intermediate hosts, including humans. Several pathways leading to the suppression of host immune response and the survival of the cysts in various hosts are known. Immune response modulation and regulated cell death (RCD) play a fundamental role in cyst formation, development and pathogenesis. RCD, referring to apoptosis, necrosis and autophagy, can be triggered either via intrinsic or extrinsic cell stimuli. In this review, we provide a general overview of current knowledge on the process of RCD during echinococcosis. The study of interactions between RCD and Echinococcus spp. metacestodes may provide in-depth understanding of echinococcosis pathogenesis and open new horizons for human intervention and treatment of the disease.

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Calmodulin-binding proteins: A journey of 40 years

Cited by 50 publications

References 96 publications

In Depth Analysis of Kinase Cross Screening Data to Identify CAMKK2 Inhibitory Scaffolds

In Depth Analysis of Kinase Cross Screening Data to Identify CAMKK2 Inhibitory Scaffolds

Calmodulin Mutations Associated with Heart Arrhythmia: A Status Report

Interactions between hydatid cyst and regulated cell death may provide new therapeutic opportunities

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