## Abstract Particularly __i__nteresting __n__ew __c__ysteineβ__h__istidineβrich protein (PINCH) is a LIMβdomainβonly adaptor protein involved in protein recruitment, subsequent assembly of multiβprotein complexes, and subcellular localization of these complexes. PINCH is developmentally regulated
Myelin Po-protein, more than just a structural protein?
β Scribed by Marie T. Filbin; Gihan I. Tennekoon
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- English
- Weight
- 916 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0265-9247
No coin nor oath required. For personal study only.
β¦ Synopsis
The protein Po has long been proposed to be responsible for the compact nature of peripheral myelin through interactions of both its extracellular and cytoplasmic domains. Recent studies support such a role for Po's extracellular region while more precise mapping of its adhesive domains are ongoing. As Po is a member of the immunoglobulin gene superfamily and perhaps bears the closest similarity to the ancestral molecule of this whole family, these studies may also have more general implications for adhesive interactions. In addition, although long believed to be purely an inert, structural molecule, Po has been reported to promote neurite outgrowth, which suggests a more dynamic role for this interesting molecule.
π SIMILAR VOLUMES
The homophilic adhesion of the peripheral nervous system myelin protein, Po, holds myelin compact at the extracellular leaflets. Po carries a single immunoglobulin (Ig)-like domain that is stabilized by a disulfide bond between Cys21 and Cys98. We showed previously that Po mutated at Cys21 to Ala (C