NDLI: Tubulin Stability and Decay: Mediation by Two Distinct Classes of IKP104-Binding Sites

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The Protein Journal : Volume 17, Issue 3, April 1998

The Protein Journal : Volume 17, Issue 2, February 1998

The Protein Journal : Volume 17, Issue 1, January 1998

The Protein Journal : Volume 16

Tubulin Stability and Decay: Mediation by Two Distinct Classes of IKP104-Binding Sites

Content Provider	Springer Nature Link
Author	Chaudhuri, Asish Ray Tomita, Isao Mizuhashi, Fukutaro Murata, Kyoji Ludueña, Richard F.
Copyright Year	1998
Abstract	IKP104, a novel antimitotic drug, has two classes of binding sites on bovine brain tubulin with different affinities. IKP104, by itself, enhances the decay of tubulin, but in the presence of colchicine or podophyllotoxin, it stabilizes tubulin instead of opening up the hydrophobic areas [Luduena et al. (1995), Biochemistry 34, 15751–15759], Here, we have dissected these two apparently contradictory effects of IKP104 by cleaving the C-terminal ends of both α and β subunits of tubulin with subtilisin. We have found that the selective removal of the C-terminal ends from both the α and β subunits of αβ tubulin lowers the sulfhydryl titer by approximately 1.5 mol/mol of dimer. Interestingly, IKP104 does not increase either the sulfhydryl liter or the exposure of hydrophobic areas of this subtilisin-treated tubulin (α$_{s}$β$_{s}$). Moreover, IKP104 lowers the sulfhydryl titer of α$_{s}$β$_{s}$ tubulin approximately by 1 mol/mol and appears to inhibit completely the time-dependent decay of α$_{s}$β$_{s}$ tubulin. The cleavage at the C-terminal ends of both α and β modulates the effect of IKP104 on the β subunit, but not on the α subunit. Fluorometric binding data analysis suggests that IKP104 binds to the α$_{s}$β$_{s}$ tubulin only at the high-affinity site; the low-affinity site(s) disappear almost completely. The sulfhydryl titer data for α and β and the fluoromelric data therefore suggest that the interaction of IKP104 at the high-affinity site on tubulin is not regulated by the C-terminal domains of α and β and the effect of the high-affinity site is restricted largely to the α subunit, while the low-affinity-site binding is modulated by the C-terminal domain of β. It also appears that the stabilization and the acceleration of the decay of tubulin are mediated by distinct interactions of IKP104 with its high- and low-affinity sites on tubulin, respectively.
Starting Page	303
Ending Page	309
Page Count	7
File Format	PDF
ISSN	02778033
Journal	The Protein Journal
Volume Number	17
Issue Number	4
e-ISSN	15734943
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	1998-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Organic Chemistry Bioorganic Chemistry Biochemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Biochemistry

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