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PMID: 18203753 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Effect of spastic paraplegia mutations in KIF5A kinesin on transport activity.

Human molecular genetics ·Vol. 17 ·No. 9 ·2008-05-01 ·Pages 1245-52

Ebbing B, Mann K, Starosta A, Jaud J, Schöls L, Schüle R, Woehlke G

Abstract

Hereditary spastic paraplegia (HSP) is a neurodegenerative disease caused by motoneuron degeneration. It is linked to at least 30 loci, among them SPG10, which causes dominant forms and originates in point mutations in the neuronal Kinesin-1 gene (KIF5A). Here, we investigate the motility of KIF5A and four HSP mutants. All mutations are single amino-acid exchanges and located in kinesin's motor or neck domain. The mutation in the neck (A361V) did not change the gliding properties in vitro, the others either reduced microtubule affinity or gliding velocity or both. In laser-trapping assays, none of the mutants moved more than a few steps along microtubules. Motility assays with mixtures of homodimeric wild-type, homodimeric mutant and heterodimeric wild-type/mutant motors revealed that only one mutant (N256S) reduces the gliding velocity at ratios present in heterozygous patients, whereas the others (K253N, R280C) do not. Attached to quantum dots as artificial cargo, mixtures involving N256S mutants produced slower cargo populations lagging behind in transport, whereas mixtures with the other mutants led to populations of quantum dots that rarely bound to microtubules. These differences indicate that the dominant inheritance of SPG10 is caused by two different mechanisms that both reduce the gross cargo flux, leading to deficient supply of the synapse.

MeSH Terms
Amino Acid Sequence Animals Biological Transport Cell Movement Genes, Dominant Heterozygote Humans Kinesins/chemistry,genetics,isolation & purification,metabolism Microtubules/physiology Molecular Motor Proteins/chemistry,genetics,isolation & purification,metabolism Mutation, Missense Point Mutation Protein Structure, Tertiary Quantum Dots Spastic Paraplegia, Hereditary/genetics Swine
Chemicals
KIF5B protein, human Molecular Motor Proteins Kinesins
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Ebbing Bettina
Institute for Cell Biology, University of Munich, Schillerstr. 42, D-80336 Munich, Germany. bettina.ebbing@lrz.uni-muenchen.de
Mann Klaudiusz
Starosta Agata
Jaud Johann
Schöls Ludger
Schüle Rebecca
Woehlke Günther
Article Info
Journal
Human molecular genetics
Abbr.
Hum Mol Genet
ISSN
1460-2083
Published
2008-05-01
Epub
2008-00-18
Pages
1245-52
Language
English
Region
England
NLM ID
9208958
Subset
IM
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