Ionic protein–lipid interaction at the plasma membrane: what can the charge do?

Li, Lunyi; Shi, Xiaoshan; Guo, Xingdong; Li, Hua; Xu, Chenqi

doi:10.1016/j.tibs.2014.01.002

Cited by 105 publications

(98 citation statements)

References 90 publications

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“…This suggests that the intact K-rich domain is required for interactions with polyacidic phospholipids in different membranes and that the specific phospholipid composition in a given membrane might determine D6PK recruitment to different membranes. The D6PK interaction with multiple polyacidic phospholipids through ionic interactions resembles previously reported mechanisms for proteinphospholipid ionic interactions and is distinct from interactions mediated between phospholipids and globular protein domains (Hammond and Balla, 2015;Li et al, 2014).…”

Section: Discussionsupporting

confidence: 73%

Phospholipid composition and a polybasic motif determine D6 PROTEIN KINASE polar association with the plasma membrane and tropic responses

et al. 2016

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Polar transport of the phytohormone auxin through PIN-FORMED (PIN) auxin efflux carriers is essential for the spatiotemporal control of plant development. The Arabidopsis thaliana serine/threonine kinase D6 PROTEIN KINASE (D6PK) is polarly localized at the plasma membrane of many cells where it colocalizes with PINs and activates PIN-mediated auxin efflux. Here, we show that the association of D6PK with the basal plasma membrane and PINs is dependent on the phospholipid composition of the plasma membrane as well as on the phosphatidylinositol phosphate 5-kinases PIP5K1 and PIP5K2 in epidermis cells of the primary root. We further show that D6PK directly binds polyacidic phospholipids through a polybasic lysine-rich motif in the middle domain of the kinase. The lysine-rich motif is required for proper PIN3 phosphorylation and for auxin transport-dependent tropic growth. Polybasic motifs are also present at a conserved position in other D6PK-related kinases and required for membrane and phospholipid binding. Thus, phospholipid-dependent recruitment to membranes through polybasic motifs might not only be required for D6PK-mediated auxin transport but also other processes regulated by these, as yet, functionally uncharacterized kinases.

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Section: Discussionsupporting

confidence: 73%

Phospholipid composition and a polybasic motif determine D6 PROTEIN KINASE polar association with the plasma membrane and tropic responses

et al. 2016

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“…These and other domains play critical roles in cell processes such as endocytosis, motility, and cytoskeletal anchoring (35,69,70). They use different mechanisms for PI(4,5)P 2 recognition, but a common theme is the presence of basic residues that bind to the negatively charged PI(4,5)P 2 (71). Our results add further evidence to the notion that bacteria have evolved mechanisms to co-opt this elaborate localization system.…”

Section: Discussionsupporting

confidence: 64%

A Novel Phosphatidylinositol 4,5-Bisphosphate Binding Domain Mediates Plasma Membrane Localization of ExoU and Other Patatin-like Phospholipases

Tyson¹,

Halavaty

Kim

et al. 2015

Journal of Biological Chemistry

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Background:The Pseudomonas aeruginosa cytotoxin ExoU localizes to the plasma membrane in eukaryotic cells. Results: ExoU and related proteins utilize a conserved four-helical bundle to bind the lipid phosphatidylinositol 4,5-bisphosphate for localization. Conclusion:The membrane localization domain of ExoU represents a novel phosphoinositide binding domain. Significance: This is the first report of a four-helical bundle with specificity for phosphatidylinositol 4,5-bisphosphate.

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“…The proposed mechanism for cell attachment is suggested to be through ionic interactions between the quaternary ammonium functional groups on the surface and oppositely charged phosphate groups present in the phospholipid bilayer of the cell membrane (Li et al 2014;Schweizer 2009). The lack of cell attachment on the negatively charged anionic cellulose films supports the suggestion that ionic interactions between scaffold and phospholipid bilayer is an important factor in cell attachment.…”

Section: Discussionmentioning

confidence: 99%

Surface modified cellulose scaffolds for tissue engineering

et al. 2016

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We report the ability of cellulose to support cells without the use of matrix ligands on the surface of the material, thus creating a two-component system for tissue engineering of cells and materials. Sheets of bacterial cellulose, grown from a culture medium containing Acetobacter organism were chemically modified with glycidyltrimethylammonium chloride or by oxidation with sodium hypochlorite in the presence of sodium bromide and 2,2,6,6-tetramethylpipiridine 1-oxyl radical to introduce a positive, or negative, charge, respectively. This modification process did not degrade the mechanical properties of the bulk material, but grafting of a positively charged moiety to the cellulose surface (cationic cellulose) increased cell attachment by 70% compared to unmodified cellulose, while negatively charged, oxidised cellulose films (anionic cellulose), showed low levels of cell attachment comparable to those seen for unmodified cellulose. Only a minimal level of cationic surface derivitisation (ca 3% degree of substitution) was required for increased cell attachment and no mediating proteins were required. Cell adhesion studies exhibited the same trends as the attachment studies, while the mean cell area and aspect ratio was highest on the cationic surfaces. Overall, we demonstrated the utility of positively charged bacterial cellulose in tissue engineering in the absence of proteins for cell attachment.

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Ionic protein–lipid interaction at the plasma membrane: what can the charge do?

Cited by 105 publications

References 90 publications

Phospholipid composition and a polybasic motif determine D6 PROTEIN KINASE polar association with the plasma membrane and tropic responses

Phospholipid composition and a polybasic motif determine D6 PROTEIN KINASE polar association with the plasma membrane and tropic responses

A Novel Phosphatidylinositol 4,5-Bisphosphate Binding Domain Mediates Plasma Membrane Localization of ExoU and Other Patatin-like Phospholipases

Surface modified cellulose scaffolds for tissue engineering

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