The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding

Dimitrios A. Skoufias, Douglas G. Cole, Karen P. Wedaman, Jonathan M. Scholey

Research output: Contribution to journalArticle

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Abstract

Sea urchin kinesin is a plus end-directed microtubule-based motor consisting of two heavy chains and two light chains and is proposed to be responsible (a) for the transport of membranous organelles along microtubules in sea urchin mitotic spindles (Wright, B. D., Henson, J. H., Wedaman, K. P., Willy, P. J., Morand, J. N., and Scholey, J. M. (1991) J. Cell Biol. 113, 817-833) and (b) for the radial dispersion of endoplasmic reticulum and endosomal membranes in non-mitotic cultured coelomocytes (Henson, J. H., Nesbitt, D., Wright, B. D., and Scholey, J. M. (1992) J. Cell Sci. 103, 309- 320). We report here that sea urchin kinesin is indeed able to bind in a concentration-dependent and saturable manner to microsomal membranes isolated from sea urchin eggs in the presence of MgATP. The kinesin light chains may not be essential for membrane binding since kinesin containing negligible amounts of light chains binds as well as kinesin containing stoichiometric amounts of light chains. Finally, we propose that kinesin binds to membranes with the carboxyl-terminal domain of the heavy chain (amino acid residues 858-1031) since the bacterially expressed and then isolated stalk-tail fragment of kinesin heavy chain, in contrast to the stalk fragment, is able (a) to bind membranes in a concentration-dependent and saturable manner and (b) to compete with native kinesin for membrane binding. Our results support the hypothesis that the carboxyl-terminal domains of the heavy chains attach kinesin molecules to their membranous cargo in mitotic and interphase sea urchin cells.

Original languageEnglish (US)
Pages (from-to)1477-1485
Number of pages9
JournalJournal of Biological Chemistry
Volume269
Issue number2
StatePublished - Jan 14 1994

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Kinesin
Membranes
Sea Urchins
Light
Microtubules
Spindle Apparatus
Interphase
Endoplasmic Reticulum
Organelles
Eggs
Tail
Adenosine Triphosphate
Amino Acids
Molecules

ASJC Scopus subject areas

  • Biochemistry

Cite this

Skoufias, D. A., Cole, D. G., Wedaman, K. P., & Scholey, J. M. (1994). The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding. Journal of Biological Chemistry, 269(2), 1477-1485.

The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding. / Skoufias, Dimitrios A.; Cole, Douglas G.; Wedaman, Karen P.; Scholey, Jonathan M.

In: Journal of Biological Chemistry, Vol. 269, No. 2, 14.01.1994, p. 1477-1485.

Research output: Contribution to journalArticle

Skoufias, DA, Cole, DG, Wedaman, KP & Scholey, JM 1994, 'The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding', Journal of Biological Chemistry, vol. 269, no. 2, pp. 1477-1485.
Skoufias DA, Cole DG, Wedaman KP, Scholey JM. The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding. Journal of Biological Chemistry. 1994 Jan 14;269(2):1477-1485.
Skoufias, Dimitrios A. ; Cole, Douglas G. ; Wedaman, Karen P. ; Scholey, Jonathan M. / The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding. In: Journal of Biological Chemistry. 1994 ; Vol. 269, No. 2. pp. 1477-1485.
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