Purified kinesin promotes vesicle motility and induces active sliding between microtubules in vitro.
AUTOR(ES)
Urrutia, R
RESUMO
We examined the ability of kinesin to support the movement of adrenal medullary chromaffin granules on microtubules in a defined in vitro system. We found that kinesin and ATP are all that is required to support efficient (33% vesicle motility) and rapid (0.4-0.6 micron/s) translocation of secretory granule membranes on microtubules in the presence of a low-salt motility buffer. Kinesin also induced the formation of microtubule asters in this buffer, with the plus ends of microtubules located at the center of each aster. This observation indicates that kinesin is capable of promoting active sliding between microtubules toward their respective plus ends, a movement analogous to that of anaphase b in the mitotic spindle. The fact that vesicle translocation, microtubule sliding, and microtubule-dependent kinesin ATPase activities are all enhanced in low-salt buffer establishes a functional parallel between this translocator and other motility ATPases, myosin, and dynein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=52156Documentos Relacionados
- Single kinesin molecules crossbridge microtubules in vitro.
- Fluctuation in the microtubule sliding movement driven by kinesin in vitro.
- Direction of active sliding of microtubules in Tetrahymena cilia.
- Simultaneous recordings of force and sliding movement between a myosin-coated glass microneedle and actin cables in vitro.
- Sliding Motility in Mycobacteria