Subcellular localization and sequence of sea urchin kinesin heavy chain: Evidence for its association with membranes in the mitotic apparatus and interphase cytoplasm

Brent D. Wright, John H. Henson, Karen P. Wedaman, Patricia J. Willy, Janice N. Morand, Jonathan M. Scholey

Research output: Contribution to journalArticle

78 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)817-833
Number of pages17
JournalJournal of Cell Biology
Volume113
Issue number4
StatePublished - May 1991

Fingerprint

Kinesin
Spindle Apparatus
Sea Urchins
Interphase
Cytoplasm
Membranes
Blastomeres
Proteins
Microtubules
Amino Acid Sequence
Embryonic Structures

ASJC Scopus subject areas

  • 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 journalArticle

Wright, Brent D. ; Henson, John H. ; Wedaman, Karen P. ; Willy, Patricia J. ; Morand, Janice N. ; Scholey, Jonathan M. / Subcellular localization and sequence of sea urchin kinesin heavy chain : Evidence for its association with membranes in the mitotic apparatus and interphase cytoplasm. In: Journal of Cell Biology. 1991 ; Vol. 113, No. 4. pp. 817-833.
@article{d372e61608e74ef19a7aaf874256d267,
title = "Subcellular localization and sequence of sea urchin kinesin heavy chain: Evidence for its association with membranes in the mitotic apparatus and interphase cytoplasm",
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.",
author = "Wright, {Brent D.} and Henson, {John H.} and Wedaman, {Karen P.} and Willy, {Patricia J.} and Morand, {Janice N.} and Scholey, {Jonathan M.}",
year = "1991",
month = "5",
language = "English (US)",
volume = "113",
pages = "817--833",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "4",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0025770088&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025770088&partnerID=8YFLogxK

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 -