Purified kinesin promotes vesicle motility and induces active sliding between microtubules in vitro

Raul Urrutia, Mark A. Mcniven, Joseph P. Albanesi, Douglas B. Murphy, Bechara Kachar

Research output: Contribution to journalArticle

104 Citations (Scopus)

Abstract

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 μm/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.

Original languageEnglish (US)
Pages (from-to)6701-6705
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number15
StatePublished - Aug 1 1991

Fingerprint

Kinesin
Microtubules
Buffers
Salts
Chromaffin Granules
Dyneins
Anaphase
Spindle Apparatus
Secretory Vesicles
Myosins
In Vitro Techniques
Adenosine Triphosphatases
Adenosine Triphosphate
Membranes

Keywords

  • Intracellular transport
  • Microtubule motility
  • Mitotic spindle dynamics
  • Organelle movement
  • Secretory granule translocation

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Purified kinesin promotes vesicle motility and induces active sliding between microtubules in vitro. / Urrutia, Raul; Mcniven, Mark A.; Albanesi, Joseph P.; Murphy, Douglas B.; Kachar, Bechara.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, No. 15, 01.08.1991, p. 6701-6705.

Research output: Contribution to journalArticle

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AU - Murphy, Douglas B.

AU - Kachar, Bechara

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AB - 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 μm/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.

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