Abstract
The Unc104/Kif1A class of kinesins transports synaptic vesicle precursors along microtubules with high speed and processivity that has been proposed to depend on reversible dimerization between two poorly motile monomers. In this issue, Al-Bassam et al. (2003) discover a structural basis for regulation of motility by reversible dimerization.
Publication types
-
Comment
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Review
MeSH terms
-
Animals
-
Axonal Transport / physiology*
-
Caenorhabditis elegans Proteins*
-
Dimerization
-
Humans
-
Models, Molecular
-
Molecular Conformation
-
Molecular Motor Proteins / chemistry*
-
Molecular Motor Proteins / physiology
-
Nerve Tissue Proteins / chemistry*
-
Nerve Tissue Proteins / physiology
-
Protein Structure, Tertiary / physiology
-
Synaptic Vesicles / physiology*
Substances
-
Caenorhabditis elegans Proteins
-
Molecular Motor Proteins
-
Nerve Tissue Proteins
-
UNC-104 protein, C elegans