Tight binding of NAP-22 with acidic membrane lipids

Maékawa, Shohei; Kobayashi, Yuumi; Morita, Mitsuhiro; Suzaki, Toshinobu

doi:10.1016/j.neulet.2015.06.025

Cited by 5 publications

(2 citation statements)

References 25 publications

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“…BASP‐1, also known as NAP‐22, is a calcium‐dependent calmodulin‐binding protein which has been involved in maturation and maintenance of synapses while GAP‐43 is expressed earlier during axonal growth (Tsuda et al ., ). These two proteins are linked to cholesterol in detergent‐resistant membrane microdomains (Maekawa et al ., ), but the interaction of BASP‐1 with cholesterol is inhibited by calmodulin in the presence of calcium (Maekawa et al ., ). It is therefore possible that the observed increase in BASP‐1 24 h after learning would not be linked to an increased synthesis but to its liberation from insoluble fractions.…”

Section: Discussionmentioning

confidence: 99%

A proteomic analysis of contextual fear conditioned rats reveals dynamic modifications in neuron and oligodendrocyte protein expression in the dentate gyrus

Houyoux

Wattiez

Ris

2017

Eur J of Neuroscience

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Contextual memory is an intricate process involving synaptic plasticity and network rearrangement. Both are governed by many molecular processes including phosphorylation and modulation of protein expression. However, little is known about the molecules involved in it. Here, we exploited the advantages of a quantitative proteomic approach to identify a great number of molecules in the rat dentate gyrus after a contextual fear conditioning session. Our results allowed us to highlight protein expression patterns, not only related to neuroplasticity, but also to myelin structure, such as myelin basic protein and myelin proteolipid protein showing a decrease in expression. Validation of the modification in protein expression reveals a dynamic profile during the 48 h following the fear conditioning session. The expression of proteins involved in neurite outgrowth, such as BASP-1 and calcineurin B1, and in synaptic structure and function, VAMP2 and RAB3C, was increased in the dentate gyrus of rats submitted to fear conditioning compared to controls. We showed that the increase in BASP-1 protein was specific to fear conditioning learning as it was not present in immediate-shock rats, neither in rats exposed to a novel environment without being shocked. As myelin is known to stabilise synaptic network, the decrease in myelin proteins suggests a neuroglia interactive process taking place in the dentate gyrus in the 24 h following contextual fear learning, which has never been demonstrated before. These results therefore open the way to the study of new plasticity mechanisms underlying learning and memory.

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Section: Discussionmentioning

confidence: 99%

A proteomic analysis of contextual fear conditioned rats reveals dynamic modifications in neuron and oligodendrocyte protein expression in the dentate gyrus

Houyoux

Wattiez

Ris

2017

Eur J of Neuroscience

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“…The low resolution also often prevents identification of both lipid class (head group) and chain length. A more routine approach to identifying the presence of lipid in complex with membrane proteins is through global size measurements such as analytical ultracentrifugation (AUC) 11, native polyacrylamide gel electrophoresis (PAGE) 12 or hyphenated approaches such as size exclusion chromatography (SEC) coupled to multi-angle light scattering (SEC-MALS) 13. In these approaches, the relative proportions of protein, lipid and detergent can be estimated which in turn can provide evidence for co-purified lipid.…”

Section: Introductionmentioning

confidence: 99%

Identifying key membrane protein lipid interactions using mass spectrometry

et al. 2018

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With the recent success in determining membrane protein structures, further detailed understanding of the identity and function of the bound lipidome is essential. Using an approach that combines high-energy native mass spectrometry (HE-nMS) and solution-phase lipid profiling, this protocol can be used to determine the identity of the endogenous lipids that directly interact with a protein. Furthermore, this method can identify systems in which such lipid binding has a major role in regulating the oligomeric assembly of membrane proteins. The protocol begins with recording of the native mass spectrum of the protein of interest, under successive delipidation conditions, to determine whether delipidation leads to disruption of the oligomeric state. Subsequently, we propose using a bipronged strategy: first, an HE-nMS platform is used that allows dissociation of the detergent micelle at the front end of the instrument. This allows for isolation of the protein-lipid complex at the quadrupole and successive fragmentation at the collision cell, which leads to identification of the bound lipid masses. Next, simultaneous coupling of this with in-solution LC-MS/MS-based identification of extracted lipids reveals the complete identity of the interacting lipidome that copurifies with the proteins. Assimilation of the results of these two sets of experiments divulges the complete identity of the set of lipids that directly interact with the membrane protein of interest, and can further delineate its role in maintaining the oligomeric state of the protein. The entire procedure takes 2 d to complete.

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