Abstract
Kinesin was previously immunolocalized to mitotic apparatuses (MAs) of early sea urchin blastomeres (Scholey, J. M., M. E. Porter, P. M. Grissom, and J. R. McIntosh. 1985. Nature [Lond.]. 318:483-486). Here we report evidence that this MA-associated motor protein is a conventional membrane-bound kinesin, rather than a kinesin-like protein. Our evidence includes the observation that the deduced amino acid sequence of this sea urchin kinesin heavy chain is characteristic of a conventional kinesin. In addition, immunolocalizations using antibodies that distinguish kinesin from kinesin-like proteins confirm that conventional kinesin is concentrated in MAs. Finally, our immunocytochemical data further suggest that conventional kinesin is associated with membranes which accumulate in MAs and interphase asters of early sea urchin embryos, and with vesicles that are distributed in the perinuclear region of coelomocytes. Thus kinesin may function as a microtubule-based vesicle motor in some MAs, as well as in the interphase cytoplasm.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 817-833 |
| Number of pages | 17 |
| Journal | Journal of Cell Biology |
| Volume | 113 |
| Issue number | 4 |
| State | Published - May 1991 |
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- Cell Biology
Cite this
Subcellular localization and sequence of sea urchin kinesin heavy chain : Evidence for its association with membranes in the mitotic apparatus and interphase cytoplasm. / Wright, Brent D.; Henson, John H.; Wedaman, Karen P.; Willy, Patricia J.; Morand, Janice N.; Scholey, Jonathan M.
In: Journal of Cell Biology, Vol. 113, No. 4, 05.1991, p. 817-833.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Subcellular localization and sequence of sea urchin kinesin heavy chain
T2 - Evidence for its association with membranes in the mitotic apparatus and interphase cytoplasm
AU - Wright, Brent D.
AU - Henson, John H.
AU - Wedaman, Karen P.
AU - Willy, Patricia J.
AU - Morand, Janice N.
AU - Scholey, Jonathan M.
PY - 1991/5
Y1 - 1991/5
N2 - Kinesin was previously immunolocalized to mitotic apparatuses (MAs) of early sea urchin blastomeres (Scholey, J. M., M. E. Porter, P. M. Grissom, and J. R. McIntosh. 1985. Nature [Lond.]. 318:483-486). Here we report evidence that this MA-associated motor protein is a conventional membrane-bound kinesin, rather than a kinesin-like protein. Our evidence includes the observation that the deduced amino acid sequence of this sea urchin kinesin heavy chain is characteristic of a conventional kinesin. In addition, immunolocalizations using antibodies that distinguish kinesin from kinesin-like proteins confirm that conventional kinesin is concentrated in MAs. Finally, our immunocytochemical data further suggest that conventional kinesin is associated with membranes which accumulate in MAs and interphase asters of early sea urchin embryos, and with vesicles that are distributed in the perinuclear region of coelomocytes. Thus kinesin may function as a microtubule-based vesicle motor in some MAs, as well as in the interphase cytoplasm.
AB - Kinesin was previously immunolocalized to mitotic apparatuses (MAs) of early sea urchin blastomeres (Scholey, J. M., M. E. Porter, P. M. Grissom, and J. R. McIntosh. 1985. Nature [Lond.]. 318:483-486). Here we report evidence that this MA-associated motor protein is a conventional membrane-bound kinesin, rather than a kinesin-like protein. Our evidence includes the observation that the deduced amino acid sequence of this sea urchin kinesin heavy chain is characteristic of a conventional kinesin. In addition, immunolocalizations using antibodies that distinguish kinesin from kinesin-like proteins confirm that conventional kinesin is concentrated in MAs. Finally, our immunocytochemical data further suggest that conventional kinesin is associated with membranes which accumulate in MAs and interphase asters of early sea urchin embryos, and with vesicles that are distributed in the perinuclear region of coelomocytes. Thus kinesin may function as a microtubule-based vesicle motor in some MAs, as well as in the interphase cytoplasm.
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M3 - Article
C2 - 1827446
AN - SCOPUS:0025770088
VL - 113
SP - 817
EP - 833
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 4
ER -