Dynamic properties of a reconstituted myelin sheath

Knoll, Wiebke; Natali, Francesca; Peters, Judith; Nanekar, Rahul; Wang, C.; Kursula, Petri

doi:10.1155/2010/317525

Cited by 23 publications

(27 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Left: the C-shaped particle seen in electron microscopy of MBP bound to lipid monolayers [24]. [48]. The structures are shown on the same scale, and the maximal dimension of MBP in each case is indicated.…”

Section: Basic Proteins Of Myelinmentioning

confidence: 99%

See 1 more Smart Citation

Myelin‐specific proteins: A structurally diverse group of membrane‐interacting molecules

et al. 2013

View full text Add to dashboard Cite

The myelin sheath is a multilayered membrane in the nervous system, which has unique biochemical properties. Myelin carries a set of specific high-abundance proteins, the structure and function of which are still poorly understood. The proteins of the myelin sheath are involved in a number of neurological diseases, including autoimmune diseases and inherited neuropathies. In this review, we briefly discuss the structural properties and functions of selected myelin-specific proteins (P0, myelin oligodendrocyte glycoprotein, myelin-associated glycoprotein, myelin basic protein, myelin-associated oligodendrocytic basic protein, P2, proteolipid protein, peripheral myelin protein of 22 kDa, 2',3'-cyclic nucleotide 3'-phosphodiesterase, and periaxin); such properties include, for example, interactions with lipid bilayers and the presence of large intrinsically disordered regions in some myelin proteins. A detailed understanding of myelin protein structure and function at the molecular level will be required to fully grasp their physiological roles in the myelin sheath.

show abstract

Section: Basic Proteins Of Myelinmentioning

confidence: 99%

“…The palmitate molecule bound to P2 in the crystal structure is also shown (blue). [48]. A predicted model, using the OPM server [27], for the binding of P2 onto one membrane surface can be seen in Fig.…”

Section: Basic Proteins Of Myelinmentioning

confidence: 99%

Myelin‐specific proteins: A structurally diverse group of membrane‐interacting molecules

et al. 2013

View full text Add to dashboard Cite

show abstract

“…Previous neutron scattering studies have shown that P2 bound to myelinmimicking vesicles made either of 1,2-dimyristoyl-snglycero-3-phosphatidic acid (DMPA) or of a binary mixture of 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS) and 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), respectively, reduces the lipid dynamics [13].…”

Section: Introductionmentioning

confidence: 99%

Neutron scattering studies on protein dynamics using the human myelin peripheral membrane protein P2

Laulumaa

Kursula

Natali

2015

EPJ Web of Conferences

View full text Add to dashboard Cite

Abstract. Myelin is a multilayered proteolipid membrane structure surrounding selected axons in the vertebrate nervous system, which allows the rapid saltatory conduction of nerve impulses. Deficits in myelin formation and maintenance may lead to chronic neurological disease. P2 is an abundant myelin protein from peripheral nerves, binding between two apposing lipid bilayers. We studied the dynamics of the human myelin protein P2 and its mutated P38G variant in hydrated powders using elastic incoherent neutron scattering. The local harmonic vibrations at low temperatures were very similar for both samples, but the mutant protein had increased flexibility and softness close to physiological temperatures. The results indicate that a drastic mutation of proline to glycine at a functional site can affect protein dynamics, and in the case of P2, they may explain functional differences between the two proteins.

show abstract

“…Here, we used the peripheral membrane protein P2 from the PNS myelin major dense line as a model system to study myelin-like membrane stack formation and structure. P2 interacts with lipid bilayers with high affinity 13,15,56–58 . We explored its membrane binding characteristics, determinants, and dynamics more closely.…”

Section: Resultsmentioning

confidence: 99%

“…Upon the formation of a P2-membrane complex, the dynamics of both the protein and lipid components are altered. When bound to P2, the dynamics of the lipid membrane are decreased 56 , while P2 becomes extremely heat-stable when bound to membranes 15 . These observations are likely to be linked to the synergistic effects of P2 and the lipids in the tightening of the 3D molecular assembly, as shown by X-ray diffraction from myelin-mimicking bicelle complexes.…”

Section: Discussionmentioning

confidence: 99%

Determinants for forming a supramolecular myelin-like proteolipid lattice

Ruskamo

Krokengen

Kowal

et al. 2020

Preprint

View full text Add to dashboard Cite

Myelin protein P2 is a peripheral membrane protein of the fatty acid binding protein family. It functions in the formation and maintenance of the peripheral nerve myelin sheath, and several P2 mutations causing human Charot-Marie-Tooth neuropathy have been reported. Here, electron cryomicroscopy of myelin-like proteolipid multilayers revealed a three-dimensionally ordered lattice of P2 molecules between stacked lipid bilayers, visualizing its possible assembly at the myelin major dense line. A single layer of P2 is inserted between two bilayers in a tight intermembrane space of ∼3 nm, implying direct interactions between P2 and two membrane surfaces. Further details on lateral protein organization were revealed through X-ray diffraction from bicelles stacked by P2. Surface mutagenesis of P2 coupled to structural and functional experiments revealed a role for both the portal region and the opposite face of P2 in membrane interactions. Atomistic molecular dynamics simulations of P2 on myelin-like and model membrane surfaces suggested that Arg88 is an important residue for P2-membrane interactions, in addition to the helical lid domain on the opposite face of the molecule. Negatively charged myelin lipid headgroups anchor P2 stably on the bilayer surface. Membrane binding may be accompanied by opening of the P2 β barrel structure and ligand exchange with the apposing lipid bilayer. Our results provide an unprecedented view into an ordered, multilayered biomolecular membrane system induced by the presence of a peripheral membrane protein from human myelin. This is an important step towards deciphering the 3-dimensional assembly of a mature myelin sheath at the molecular level.

show abstract

Dynamic properties of a reconstituted myelin sheath

Cited by 23 publications

References 27 publications

Myelin‐specific proteins: A structurally diverse group of membrane‐interacting molecules

Myelin‐specific proteins: A structurally diverse group of membrane‐interacting molecules

Neutron scattering studies on protein dynamics using the human myelin peripheral membrane protein P2

Determinants for forming a supramolecular myelin-like proteolipid lattice

Contact Info

Product

Resources

About