Genomics | Cognitive Neuroscience | Control of Gene Expression | Bone Biology, Osteoporosis & Other Diseases of Bone | Neuromuscular Diseases
Strumpellin is a novel VCP/p97-binding protein linking hereditary spastic paraplegia to protein aggregation diseases
Karthikeyan Tangavelou, Christoph S Clemen*, Karl-Heinz Strucksberg, Steffen Just, Linda Gaertner, Jens Reimann, Rolf Schröder
*Corresponding author: Christoph S Clemen
Institute of Biochemistry I, Center for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany
F1000Posters 2011, 2: 5 (poster) [ENGLISH]
Poster [2.27 MB]
Presented at
American Society for Cell Biology Annual Meeting 2010 ,
11 - 15 Dec 2010, 718
Mutations of the human valosin-containing protein gene cause autosomal-dominant inclusion body myopathy associated with Paget’s disease of bone and frontotemporal dementia. We identified strumpellin as a novel valosin-containing protein binding partner.
Strumpellin mutations have been shown to cause hereditary spastic paraplegia. We demonstrate that strumpellin is a ubiquitously expressed protein present in cytosolic and endoplasmic reticulum cell fractions.
Our data implies a strumpellin loss-of-function pathogenesis in hereditary spastic paraplegia. In the human central nervous system strumpellin shows a presynaptic localization. We further identified strumpellin in pathological protein aggregates in inclusion body myopathy associated with Paget’s disease of bone and frontotemporal dementia, and various myofibrillar myopathies. Beyond hereditary spastic paraplegia, our findings imply that mutant forms of strumpellin and valosin-containing protein may have a concerted pathogenic role in protein aggregate diseases.
No relevant conflicts of interest declared.
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