The Binding Properties and Physiological Functions of Recoverin

Zang, Jingjing; Neuhauss, Stephan C. F.

doi:10.3389/fnmol.2018.00473

Cited by 35 publications

(31 citation statements)

References 96 publications

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“…Probably PYGM is involved in the inactivation, recovery, and/or regulation of the phototransduction cascade through interaction with recoverin (RCVRN) and CALM1, both connected with Ca 2+ cellular level regulation. The RCVRN, a low-molecular-weight, neuronal calcium sensor, is involved in phototransduction cascade regulation and signal transmission in a calcium-dependent manner [ 32 , 35 ]. So far, no experimental data explain the exact role of PYGM in this process.…”

Section: The Biological Importance Of Pygmmentioning

confidence: 99%

Muscle Glycogen Phosphorylase and Its Functional Partners in Health and Disease

Migocka-Patrzałek

Elías

2021

Cells

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Glycogen phosphorylase (PG) is a key enzyme taking part in the first step of glycogenolysis. Muscle glycogen phosphorylase (PYGM) differs from other PG isoforms in expression pattern and biochemical properties. The main role of PYGM is providing sufficient energy for muscle contraction. However, it is expressed in tissues other than muscle, such as the brain, lymphoid tissues, and blood. PYGM is important not only in glycogen metabolism, but also in such diverse processes as the insulin and glucagon signaling pathway, insulin resistance, necroptosis, immune response, and phototransduction. PYGM is implicated in several pathological states, such as muscle glycogen phosphorylase deficiency (McArdle disease), schizophrenia, and cancer. Here we attempt to analyze the available data regarding the protein partners of PYGM to shed light on its possible interactions and functions. We also underline the potential for zebrafish to become a convenient and applicable model to study PYGM functions, especially because of its unique features that can complement data obtained from other approaches.

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Section: The Biological Importance Of Pygmmentioning

confidence: 99%

Muscle Glycogen Phosphorylase and Its Functional Partners in Health and Disease

Migocka-Patrzałek

Elías

2021

Cells

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“…Unveiling the detailed structural mechanisms underlying the Rec function may lead to useful generalizations to other NCS proteins, considering the prototypical role of Rec as a myristoyl-switch protein [2]. A number of experimental studies based on NMR [5,28,38,45], surface plasmon resonance [7,12,46,47] and dynamic light scattering [48,49] all confirmed that the binding of two Ca 2+ ions to the functional motifs EF2 and EF3 in Rec triggers the myristoyl switch process, which by extruding the acyl chain from the protein milieu leads to the significant exposure of a hydrophobic crevice eventually necessary to accommodate the GRK1 target.…”

Section: Discussionmentioning

confidence: 99%

“…The small (23 kDa) Ca 2+ -binding protein recoverin (Rec) is a prototypical member of the neuronal calcium sensor (NCS) family mostly expressed in vertebrate photoreceptors, where it plays a role in the regulation of the phototransduction cascade [1,2]. Light triggers a transient drop in the intracellular concentration of Ca 2+ and such change is promptly detected by a group of calcium sensors including Rec, which reversibly bind to specific targets in a Ca 2+ -dependent manner.…”

Section: Introductionmentioning

confidence: 99%

Effects of Membrane and Biological Target on the Structural and Allosteric Properties of Recoverin: A Computational Approach

Borsatto

Marino

Abrusci

et al. 2019

IJMS

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Recoverin (Rec) is a prototypical calcium sensor protein primarily expressed in the vertebrate retina. The binding of two Ca2+ ions to the functional EF-hand motifs induces the extrusion of a myristoyl group that increases the affinity of Rec for the membrane and leads to the formation of a complex with rhodopsin kinase (GRK1). Here, unbiased all-atom molecular dynamics simulations were performed to monitor the spontaneous insertion of the myristoyl group into a model multicomponent biological membrane for both isolated Rec and for its complex with a peptide from the GRK1 target. It was found that the functional membrane anchoring of the myristoyl group is triggered by persistent electrostatic protein-membrane interactions. In particular, salt bridges between Arg43, Arg46 and polar heads of phosphatidylserine lipids are necessary to enhance the myristoyl hydrophobic packing in the Rec-GRK1 assembly. The long-distance communication between Ca2+-binding EF-hands and residues at the interface with GRK1 is significantly influenced by the presence of the membrane, which leads to dramatic changes in the connectivity of amino acids mediating the highest number of persistent interactions (hubs). In conclusion, specific membrane composition and allosteric interactions are both necessary for the correct assembly and dynamics of functional Rec-GRK1 complex.

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“…It is a unique protein that uses a calcium–acyl switch for regulated membrane attachment and probable association with interactors similar to the protein recoverin. Recoverin is a neuronal calcium sensor, mainly expressed in retinal photoreceptors [81,82]. It is myristoylated in the calcium-bound state and associates with the plasma membrane via interactors.…”

Section: Double Acylation: Myristoylation and Palmitoylationmentioning

confidence: 99%

Lipid Modifications in Cilia Biology

Roy

Marin

2019

JCM

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Cilia are specialized cellular structures with distinctive roles in various signaling cascades. Ciliary proteins need to be trafficked to the cilium to function properly; however, it is not completely understood how these proteins are delivered to their final localization. In this review, we will focus on how different lipid modifications are important in ciliary protein trafficking and, consequently, regulation of signaling pathways. Lipid modifications can play a variety of roles, including tethering proteins to the membrane, aiding trafficking through facilitating interactions with transporter proteins, and regulating protein stability and abundance. Future studies focusing on the role of lipid modifications of ciliary proteins will help our understanding of how cilia maintain specific protein pools strictly connected to their functions.

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The Binding Properties and Physiological Functions of Recoverin

Cited by 35 publications

References 96 publications

Muscle Glycogen Phosphorylase and Its Functional Partners in Health and Disease

Muscle Glycogen Phosphorylase and Its Functional Partners in Health and Disease

Effects of Membrane and Biological Target on the Structural and Allosteric Properties of Recoverin: A Computational Approach

Lipid Modifications in Cilia Biology

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