Transmembrane domain of myelin protein zero can form dimers: Possible implications for myelin construction
SCIE
SCOPUS
- Title
- Transmembrane domain of myelin protein zero can form dimers: Possible implications for myelin construction
- Authors
- Plotkowski, ML; Kim, S; Phillips, ML; Partridge, AW; Deber, CM; Bowie, JU
- Date Issued
- 2007-10-30
- Publisher
- AMER CHEMICAL SOC
- Abstract
- Myelin protein zero (MPZ) is the major integral membrane protein of peripheral nerve myelin in higher vertebrates, mediating homoadhesion of the multiple, spiraling wraps of the myelin sheath. Previous studies have shown that full-length MPZ can form dimers and tetramers, and biochemical studies on the extracellular domain (ECD) indicate that it can form a tetramer, albeit very weakly. On the basis of cross-linking studies and equilibrium sedimentation of a transmembrane (TM) domain peptide (MP-ZTM), we find that the MPZ-TM can form homodimers. We further characterized the dimer by measuring the effects of alanine and leucine substitutions on the ability of the TM to dimerize in Escherichia coli membranes. Our results indicate that the primary packing interface for the MPZ TM homodimer is a glycine zipper (GxxxGxxxG) motif. We also find that the G134R mutation, which lies within the glycine zipper packing interface and causes Charcot-Marie-Tooth disease type 1B, severely inhibits dimerization, suggesting that dimerization of the TM domain may be important for the normal functioning of MPZ. By combining our new results with prior work, we suggest a new model for an MPZ lattice that may form during the construction of myelin.
- Keywords
- MAJOR STRUCTURAL PROTEIN; MARIE-TOOTH-DISEASE; EXTRACELLULAR DOMAIN; PERIPHERAL MYELIN; MEMBRANE-PROTEINS; DEJERINE-SOTTAS; NERVE MYELIN; MUTATIONS; GLYCOPROTEIN; NEUROPATHY
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/23110
- DOI
- 10.1021/BI701066H
- ISSN
- 0006-2960
- Article Type
- Article
- Citation
- BIOCHEMISTRY, vol. 46, no. 43, page. 12164 - 12173, 2007-10-30
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.