Interaction of the cytoskeletal component vinculin with bilayer structures analyzed with a photoactivatable phospholipid.

Niggli, Verena; Dimitrov, Dimitar; Brunner, Josef; Burger, Max M.

doi:10.1016/s0021-9258(19)62703-1

Cited by 69 publications

(18 citation statements)

References 31 publications

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“…PIP 2 binds to two discrete sequence stretches in the vinculin tail, thereby disrupting the head-tail interaction and inducing oligomerization of vinculin. Electron microscopic data have already demonstrated the formation of vinculin oligomers by tail-tail interactions [35], and photo-crosslinking studies with liposomes have suggested that vinculin oligomerizes as the result of its interaction with acidic phospholipids [36]. The PIP 2 -binding sites, as identified in this study, coincide with two regions of predicted amphipathic helices [37] that are also involved in F-actin…”

Section: Discussionsupporting

confidence: 68%

The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate

et al. 1998

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Focal contact assembly involves interaction between VASP and vinculin, which is enhanced by PIP2-induced vinculin activation and oligomerization. Given that vinculin and VASP both bind to F-actin, vinculin-VASP complexes might bundle the distal ends of actin filaments in focal contacts. We propose that PIP2-dependent signalling modulates microfilament organization at cellular adhesion sites by regulating vinculin-VASP complexes.

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Section: Discussionsupporting

confidence: 68%

The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate

et al. 1998

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“…So far, most of the attention in the field of cytoskeletonplasma membrane interaction has been paid to the interaction between cytoskeleton proteins and membrane receptors [for a review, see Luna and Hitt (1992)]. However, recently many cytoskeleton proteins, such as actin (St-Onge & Gicquaud, 1990), spectrin (Cohen et al, 1986), vinculin (Niggli et al, 1986), myosin I (Hayden et al, 1990, band 4.1 (Sato & Ohnishi, 1983), synapsin I (Benfenati et al, 1989), and R-actinin, etc., have been found to be able to interact directly with negatively charged phospholipids. These proteins have been categorized as the amphitropic proteins by Burn (1988).…”

Section: Discussionmentioning

confidence: 99%

Interactions between Smooth Muscle α-Actinin and Lipid Bilayers

Han

Kang

1997

Biochemistry

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alpha-Actinin has been proposed to be the actin-plasma membrane linker. This assumption is based on the discovery of direct interaction of alpha-actinin with two specific lipids, diacylglycerol and palmitic acid [Burn, P. (1988) Trends Biochem. Sci. 13, 79-83]. In our study, the binding of alpha-actinin with vesicles containing negatively charged phospholipids was measured by the method of 90 degrees light-scattering. Our results show that alpha-actinin is able to bind membranes containing negatively charged phospholipids, but not to bind membranes composed of neutral lipids only. Diacylglycerol and palmitic acid, on the other hand, have little effect on the binding of alpha-actinin to lipid vesicles. Analysis of binding isotherms in terms of a membrane binding model gave apparent dissociation constants which varied between 0.2 and 3 microM over a range of 5-20 mol % negatively charged phospholipid. Comparing the kinetics of alpha-chymotrypsin digestion of alpha-actinin in solution to those of vesicle-bound alpha-actinin, it can be seen that the cleavage site at the junction between the C-terminal and the central rod domain of alpha-actinin and another cleavage site on the C-terminal domain can be most effectively protected by its membrane binding. Analysis of the amide I and II regions of Fourier-transform infrared spectra of alpha-actinin revealed that the association of alpha-actinin with negatively charged phospholipid vesicles resulted in some perturbation of the protein secondary structure. Monolayers containing negatively charged phospholipid were layered and incubated on the surface of a polymerization solution of actin and alpha-actinin, and observed with an electron microscope. The results show that the bundle structure of actin filaments can be formed if diacylglycerol and palmitic acid are present in lipid layers.

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“…A physiological role for the interaction of apolipoproteins, surfactant-associated protein SAP-35 and several cytoskeletal proteins with phospholipids has been suggested. In the case of apolipoproteins, the lipid binding coincides with the biological activity of carrying lipids in an aqueous environment (22,31); in the case of SAP-35, it is probably involved in the extracellular organization of the surfactant phospholipids in a regular lattice on the alveolar surface (32, 49); in the case of cytoskeletal proteins, it may mediate their association with the cytoplasmic surface of the plasmalemma or of subcellular structures (28,33,47,48,50,56).…”

Section: Discussionmentioning

confidence: 99%

Electrostatic and hydrophobic interactions of synapsin I and synapsin I fragments with phospholipid bilayers.

Benfenati

Greengard

Brunner

et al. 1989

The Journal of Cell Biology

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142

123

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Abstract. Synapsin I, a major neuron-specific phosphoprotein, is localized on the cytoplasmic surface of small synaptic vesicles to which it binds with high affinity. It contains a collagenase-resistant head domain and a collagenase-sensitive elongated tail domain. In the present study, the interaction between synapsin I and phospholipid vesicles has been characterized, and the protein domains involved in these interactions have been identified. When lipid vesicles were prepared from cholesterol and phospholipids using a lipid composition similar to that found in native synaptic vesicle membranes (40% phosphatidylcholine, 32% phosphatidylethanolamine, 12% phosphatidylserine, 5% phosphatidylinositol, 10% cholesterol, wt/wt), synapsin I bound with a dissociation constant of 14 nM and a maximal binding capacity of about 160 fmol of synapsin I/#g of phospholipid. Increasing the ionic strength decreased the affinity without greatly affecting the maximal amount of synapsin I bound. When vesicles containing cholesterol and either phosphatidylcholine or phosphatidylcholine/phosphatidylethanolamine were tested, no significant binding was detected under any conditions examined. On the other hand, phosphatidylcholine vesicles containing either phosphatidylserine or phosphatidylinositol strongly interacted with synapsin I. The amount of synapsin I maximally bound was directly proportional to the percentage of acidic phospholipids present in the lipid bilayer, whereas the Kj value was not affected by varying the phospholipid composition. A study of synapsin I fragments obtained by cysteine-specific cleavage showed that the collagenase-resistant head domain actively bound to phospholipid vesicles; in contrast, the collagenasesensitive tail domain, though strongly basic, did not significantly interact. Photolabeling of synapsin I was performed with the phosphatidylcholine analogue l-palmitoyl-2- [11-[4-[3-(trifluoromethyl)] undecanoyl]-sn-glycero-3-phosphocholine; this compound generates a highly reactive carbene that selectively interacts with membrane-embedded domains of membrane proteins. Synapsin I was significantly labeled upon photolysis when incubated with lipid vesicles containing acidic phospholipids and trace amounts of the photoactivatable phospholipid. Proteolytic cleavage of photolabeled synapsin I localized the label to the head domain of the molecule. The results suggest that synapsin I, which has an amphiphilic character and local regions of positive charge, interacts withartificial membranes containing acidic phospholipids, and this surface interaction, presumably of electrostatic nature, is followed by a penetration of the head domain into the hydrophobic core of the membrane. p ROTEIN phosphorylation represents a process of paramount importance in the nervous system and is involved in signal transduction and information processing (45). Synapsin I, a collective name for two closely related peptides (Ia and Ib) with apparent molecular weights of 86,000 and 80,000 on SDS-PAGE, is a major neuronspecific phospho...

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Interaction of the cytoskeletal component vinculin with bilayer structures analyzed with a photoactivatable phospholipid.

Cited by 69 publications

References 31 publications

The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate

The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate

Interactions between Smooth Muscle α-Actinin and Lipid Bilayers

Electrostatic and hydrophobic interactions of synapsin I and synapsin I fragments with phospholipid bilayers.

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