Molecular characterization and immunohistochemical localization of palmdelphin, a cytosolic isoform of the paralemmin protein family implicated in membrane dynamics
2005 (English)In: European Journal of Cell Biology, ISSN 0171-9335, E-ISSN 1618-1298, Vol. 84, no 11, 853-866 p.Article in journal (Refereed) Published
Palmdelphin is a newly identified cytosolic isoform of paratemmin-1, a lipid raft-associated protein implicated in cell shape control. Like paralemmin- 1,palmdelphin is phosphorylated, giving rise to electrophoretic band heterogeneity that is most pronounced in the brain. In ultracentrifugation and get filtration palmdelphin behaves as a non-globular monomer. Its C-terminal region binds glutamine synthetase. Immunohistochemical analysis of the rat brain shows a prominent localization of palmdelphin in the cerebral cortex, hippocampus, amygdala, septum, indusium griseum, piriform cortex, nucleus supraopticus, and nucleus of the lateral olfactory tract. Many of the circumscript palmdelphin-positive areas are related to the olfactory system. Immunoperoxidase electron microscopy reveals a discontinuous distribution of palmdelphin immunoreactivity, in the form of spots scattered throughout the cytoplasm of selected neuronal perikarya and dendrites, including dendritic spines, often in association with endomembranes, and in a pattern which is similar to that of the cytoplasmic fraction of paralemmin-1. In subcellular fractionation experiments palmdelphin behaves as a cytosolic protein which, however, can be partially recruited from cytosol to the detergent-resistant fraction of a membrane/cytoskeletal cell ghost preparation. These observations suggest that palmdelphin may peripherally associate with endomembranes or cytoskeleton-linked structures.
Place, publisher, year, edition, pages
2005. Vol. 84, no 11, 853-866 p.
protein phosphorylation, membrane traffic, glutamine synthetase, lipid rafts, dendrite, dendritic spine
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-77816DOI: 10.1016/j.ejcb.2005.07.002ISI: 000233664900001PubMedID: 16323283OAI: oai:DiVA.org:uu-77816DiVA: diva2:105728