Moving on to the cargo problem of microtubule-dependent motors in neurons

• Published in: Current Opinion in Neurobiology Vol. 10; no. 5; pp. 566 - 573
• Main Authors: Terada, Sumio, Hirokawa, Nobutaka
• Format: Book Review Journal Article
• Language: English
• Published: England Elsevier Ltd 01.10.2000
• Subjects: Animals; Dyneins - metabolism; Dyneins - physiology; Humans; Kinesin - metabolism; Kinesin - physiology; Microtubule Proteins - metabolism; Microtubule Proteins - physiology; Microtubules - metabolism; Microtubules - physiology; Molecular Motor Proteins - metabolism; Molecular Motor Proteins - physiology; molecular motors; Neurons - metabolism; Neurons - physiology; Synaptic Transmission - physiology; GFP, green fluorescent protein; PDZ domain, PSD-95, DLG, ZO-1 domain; NMDA, N-methyl-d-aspartate; KLC, kinesin light chain; DLG, discs large; ChAT, choline acetyltransferase; COP1, coatomer protein 1; KIF5, kinesin superfamily protein 5/kinesin heavy chain; KIF, kinesin superfamily protein; CAM, cell adhesion molecule; KAP3, kinesin superfamily associated protein of KIF3; PSD-95, postsynaptic density protein of 95 kDa; ZO-1, zona occludens-1; NMDAR2B, NMDA receptor 2B
• ISSN: 0959-4388; 1873-6882
• DOI: 10.1016/S0959-4388(00)00129-X

Vigorous investigation has finally begun to shed light on the cargo problem of the microtubule-dependent motors, kinesin and dynein superfamily proteins. Biochemical observations have suggested that the potential cargoes of certain populations of motor proteins seem to be in vesicle-form, each vesicle possessing specific functional marker molecules. In addition to the close relationship between microtubule-dependent motors and cargoes in vesicle-form, kinesin has also been highlighted as an apparent driving force for another cargo in non-vesicle-form, cytoplasmic protein. On the basis of new biophysical and cell-biological evidence, the controversy over the movement of cytoplasmic cargoes has entered a new phase.