TY - JOUR
T1 - Purified kinesin promotes vesicle motility and induces active sliding between microtubules in vitro
AU - Urrutia, Raul
AU - Mcniven, Mark A.
AU - Albanesi, Joseph P.
AU - Murphy, Douglas B.
AU - Kachar, Bechara
PY - 1991/8/1
Y1 - 1991/8/1
N2 - 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.
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.
KW - Intracellular transport
KW - Microtubule motility
KW - Mitotic spindle dynamics
KW - Organelle movement
KW - Secretory granule translocation
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U2 - 10.1073/pnas.88.15.6701
DO - 10.1073/pnas.88.15.6701
M3 - Article
C2 - 1830666
AN - SCOPUS:0026009462
SN - 0027-8424
VL - 88
SP - 6701
EP - 6705
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 15
ER -