Association of Lyn kinase with membrane rafts determines its negative influence on LPS-induced signaling

Borzęcka-Solarz, Kinga; Dembińska, Justyna; Hromada-Judycka, Aneta; Traczyk, Gabriela; Ciesielska, Anna; Ziemlińska, Ewelina; Świątkowska, Anna; Kwiatkowska, Katarzyna

doi:10.1091/mbc.e16-09-0632

Cited by 19 publications

(20 citation statements)

References 69 publications

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“…Recent proteomic studies based on 17ODYA labeling of RAW264 macrophage-like cells followed by click chemistry have revealed that stimulation of cells with LPS induces profound changes of the abundance of palmitoylated proteins ( 182 ). The data are in agreement with earlier findings showing that LPS induces accumulation of S -palmitoylated Lyn kinase in the raft-enriched fraction of cells, allowing it to downregulate TLR4 signaling ( 11 ). One of the upregulated S -palmitoylated proteins was type II phosphatidylinositol 4-kinase IIβ, which phosphorylates phosphatidylinositol to phosphatidylinositol 4-monophosphate.…”

Section: Palmitoylation Of Host Proteins Involved In Antibacterial Ansupporting

confidence: 93%

“…The click chemistry-based methods can also be used to follow the cellular localization of palmitoylated proteins by immunofluorescence when combined with the proximity ligation technique ( 111 , 112 ). Palmitoylation of individual proteins can also be studied after their immunoprecipitation ( 11 , 72 , 73 , 98 ).…”

Section: Methodological Progress Facilitates Detection Of Protein Palmentioning

confidence: 99%

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Protein Palmitoylation and Its Role in Bacterial and Viral Infections

et al. 2018

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S-palmitoylation is a reversible, enzymatic posttranslational modification of proteins in which palmitoyl chain is attached to a cysteine residue via a thioester linkage. S-palmitoylation determines the functioning of proteins by affecting their association with membranes, compartmentalization in membrane domains, trafficking, and stability. In this review, we focus on S-palmitoylation of proteins, which are crucial for the interactions of pathogenic bacteria and viruses with the host. We discuss the role of palmitoylated proteins in the invasion of host cells by bacteria and viruses, and those involved in the host responses to the infection. We highlight recent data on protein S-palmitoylation in pathogens and their hosts obtained owing to the development of methods based on click chemistry and acyl-biotin exchange allowing proteomic analysis of protein lipidation. The role of the palmitoyl moiety present in bacterial lipopolysaccharide and lipoproteins, contributing to infectivity and affecting recognition of bacteria by innate immune receptors, is also discussed.

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Section: Palmitoylation Of Host Proteins Involved In Antibacterial Ansupporting

confidence: 93%

Section: Methodological Progress Facilitates Detection Of Protein Palmentioning

confidence: 99%

Protein Palmitoylation and Its Role in Bacterial and Viral Infections

et al. 2018

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“…Src family kinase Fyn, an inhibitory regulator of TLR4, is palmitoylated at Cys3, a modification required for its lipid raft localization and catalytic function. LPS stimulation increases the level of palmitoylated Fyn in lipid rafts where Fyn mediates the suppression of both NF-κB and IRF3-dependent cytokine production (Borzecka-Solarz et al, 2017). Another LPS-upregulated palmitoylated protein is type II phosphatidylinositol 4-kinase (PI4KIIB).…”

Section: Pathogen Recognition Tlr Signaling Pathwaymentioning

confidence: 99%

Protein Palmitoylation in Leukocyte Signaling and Function

Yang

Chatterjee

et al. 2020

Front. Cell Dev. Biol.

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Palmitoylation is a post-translational modification (PTM) based on thioester-linkage between palmitic acid and the cysteine residue of a protein. This covalent attachment of palmitate is reversibly and dynamically regulated by two opposing sets of enzymes: palmitoyl acyltransferases containing a zinc finger aspartate-histidine-histidine-cysteine motif (PAT-DHHCs) and thioesterases. The reversible nature of palmitoylation enables fine-tuned regulation of protein conformation, stability, and ability to interact with other proteins. More importantly, the proper function of many surface receptors and signaling proteins requires palmitoylation-meditated partitioning into lipid rafts. A growing number of leukocyte proteins have been reported to undergo palmitoylation, including cytokine/chemokine receptors, adhesion molecules, pattern recognition receptors, scavenger receptors, T cell co-receptors, transmembrane adaptor proteins, and signaling effectors including the Src family of protein kinases. This review provides the latest findings of palmitoylated proteins in leukocytes and focuses on the functional impact of palmitoylation in leukocyte function related to adhesion, transmigration, chemotaxis, phagocytosis, pathogen recognition, signaling activation, cytotoxicity, and cytokine production.

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“…Fyn, another Src-family kinase which undergoes mono-myristylation and di-palmitoylation, is directly targeted to the plasma membrane after protein synthesis [ 11 ]. These lipid modifications are important for appropriate functioning of Src-family kinases: palmitoylation is required for accumulation of Lyn to lipid rafts and the involvement of Lyn in lipopolysaccharide-induced signaling in RAW264 macrophage-like cells [ 71 ]; palmitoylation of c-Yes mediates oncogenic signaling in HT29 colorectal cancer cells [ 72 ]; the lack of lipid modifications in c-Src and Lyn causes chromosome missegregation in mitotic HeLa S3 cells [ 73 ]. Third, as with the lipid raft markers that are internalized in suspended cells, Src-family kinases can be translocated from the plasma membrane to endomembranes after loss of cell–cell or cell–scaffold interactions, the pattern of which varies among cell types ( Figure 1 b).…”

Section: Changes In the Localizations Of Src-family Kinases Upon Cmentioning

confidence: 99%

Role of Membrane Cholesterol Levels in Activation of Lyn upon Cell Detachment

Morinaga

Yamaguchi

Nakayama

et al. 2018

IJMS

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Cholesterol, a major component of the plasma membrane, determines the physical properties of biological membranes and plays a critical role in the assembly of membrane microdomains. Enrichment or deprivation of membrane cholesterol affects the activities of many signaling molecules at the plasma membrane. Cell detachment changes the structure of the plasma membrane and influences the localizations of lipids, including cholesterol. Recent studies showed that cell detachment changes the activities of a variety of signaling molecules. We previously reported that the localization and the function of the Src-family kinase Lyn are critically regulated by its membrane anchorage through lipid modifications. More recently, we found that the localization and the activity of Lyn were changed upon cell detachment, although the manners of which vary between cell types. In this review, we highlight the changes in the localization of Lyn and a role of cholesterol in the regulation of Lyn’s activation following cell detachment.

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Association of Lyn kinase with membrane rafts determines its negative influence on LPS-induced signaling

Cited by 19 publications

References 69 publications

Protein Palmitoylation and Its Role in Bacterial and Viral Infections

Protein Palmitoylation and Its Role in Bacterial and Viral Infections

Protein Palmitoylation in Leukocyte Signaling and Function

Role of Membrane Cholesterol Levels in Activation of Lyn upon Cell Detachment

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