scholarly journals The auto-inhibitory domain and ATP-independent microtubule-binding region of Kinesin heavy chain are major functional domains for transport in the Drosophila germline

Development ◽  
2013 ◽  
Vol 141 (1) ◽  
pp. 176-186 ◽  
Author(s):  
L. S. Williams ◽  
S. Ganguly ◽  
P. Loiseau ◽  
B. F. Ng ◽  
I. M. Palacios
Keyword(s):  
Heavy Chain ◽  
Functional Domains ◽  
Binding Region ◽  
Microtubule Binding ◽  
Kinesin Heavy Chain ◽  
Inhibitory Domain

scholarly journals Isolation of a 45-kDa Fragment from the Kinesin Heavy Chain with Enhanced ATPase and Microtubule-binding Activities

1989 ◽  
Vol 264 (1) ◽  
pp. 589-595
Author(s):  
S A Kuznetsov ◽  
Y A Vaisberg ◽  
S W Rothwell ◽  
D B Murphy ◽  
V I Gelfand
Keyword(s):  
Heavy Chain ◽  
Microtubule Binding ◽  
Kinesin Heavy Chain

A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses

Cell ◽  
1989 ◽  
Vol 56 (5) ◽  
pp. 879-889 ◽  
Author(s):  
Joy T. Yang ◽  
Robert A. Laymon ◽  
Lawrence S.B. Goldstein
Keyword(s):  
Domain Structure ◽  
Dna Sequence ◽  
Heavy Chain ◽  
Microtubule Binding ◽  
Kinesin Heavy Chain

Molecular Basis of Dystrobrevin Interaction with Kinesin Heavy Chain: Structural Determinants of their Binding

2005 ◽  
Vol 354 (4) ◽  
pp. 872-882 ◽  
Author(s):  
Marina Ceccarini ◽  
Paola Torreri ◽  
Dario Giuseppe Lombardi ◽  
Gianfranco Macchia ◽  
Pompeo Macioce ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Molecular Basis ◽  
Structural Determinants ◽  
Kinesin Heavy Chain

IDENTIFICATION AND PROPERTIES OF RAT BRAIN KINESIN HEAVY CHAIN ASSOCIATED WITH MITOCHONDRIA

1991 ◽  
Vol 73 (2-3) ◽  
pp. 18a-18a ◽  
Author(s):  
Abdeljelil Jellali ◽  
Irina Surgucheva ◽  
Vera Jancsik ◽  
Dominique Filliol ◽  
Alvaro Rendon
Keyword(s):  
Rat Brain ◽  
Heavy Chain ◽  
Kinesin Heavy Chain

scholarly journals A functional role for intrinsic disorder in the tau-tubulin complex

2016 ◽  
Vol 113 (50) ◽  
pp. 14336-14341 ◽  
Author(s):  
Ana M. Melo ◽  
Juliana Coraor ◽  
Garrett Alpha-Cobb ◽  
Shana Elbaum-Garfinkle ◽  
Abhinav Nath ◽  
...  
Keyword(s):  
Single Molecule ◽  
Solution Structure ◽  
Dynamic Instability ◽  
Resonance Energy ◽  
Intrinsically Disordered Protein ◽  
Conformational Ensemble ◽  
Binding Region ◽  
Global Features ◽  
Microtubule Binding ◽  
Intrinsically Disordered

Tau is an intrinsically disordered protein with an important role in maintaining the dynamic instability of neuronal microtubules. Despite intensive study, a detailed understanding of the functional mechanism of tau is lacking. Here, we address this deficiency by using intramolecular single-molecule Förster Resonance Energy Transfer (smFRET) to characterize the conformational ensemble of tau bound to soluble tubulin heterodimers. Tau adopts an open conformation on binding tubulin, in which the long-range contacts between both termini and the microtubule binding region that characterize its compact solution structure are diminished. Moreover, the individual repeats within the microtubule binding region that directly interface with tubulin expand to accommodate tubulin binding, despite a lack of extension in the overall dimensions of this region. These results suggest that the disordered nature of tau provides the significant flexibility required to allow for local changes in conformation while preserving global features. The tubulin-associated conformational ensemble is distinct from its aggregation-prone one, highlighting differences between functional and dysfunctional states of tau. Using constraints derived from our measurements, we construct a model of tubulin-bound tau, which draws attention to the importance of the role of tau’s conformational plasticity in function.

scholarly journals Clonal Tests of Conventional Kinesin Function during Cell Proliferation and Differentiation

2000 ◽  
Vol 11 (4) ◽  
pp. 1329-1343 ◽  
Author(s):  
Robert P. Brendza ◽  
Kathy B. Sheehan ◽  
F.R. Turner ◽  
William M. Saxton
Keyword(s):  
Cell Proliferation ◽  
Endoplasmic Reticulum ◽  
Heavy Chain ◽  
Larval Instar ◽  
Vesicle Transport ◽  
Ultrastructural Changes ◽  
Chain Gene ◽  
Cell Periphery ◽  
Kinesin Heavy Chain ◽  
Conventional Kinesin

Null mutations in the Drosophila Kinesin heavy chain gene (Khc), which are lethal during the second larval instar, have shown that conventional kinesin is critical for fast axonal transport in neurons, but its functions elsewhere are uncertain. To test other tissues, single imaginal cells in young larvae were rendered null for Khc by mitotic recombination. Surprisingly, the null cells produced large clones of adult tissue. The rates of cell proliferation were not reduced, indicating that conventional kinesin is not essential for cell growth or division. This suggests that in undifferentiated cells vesicle transport from the Golgi to either the endoplasmic reticulum or the plasma membrane can proceed at normal rates without conventional kinesin. In adult eye clones produced by null founder cells, there were some defects in differentiation that caused mild ultrastructural changes, but they were not consistent with serious problems in the positioning or transport of endoplasmic reticulum, mitochondria, or vesicles. In contrast, defective cuticle deposition by highly elongated Khc null bristle shafts suggests that conventional kinesin is critical for proper secretory vesicle transport in some cell types, particularly ones that must build and maintain long cytoplasmic extensions. The ubiquity and evolutionary conservation of kinesin heavy chain argue for functions in all cells. We suggest interphase organelle movements away from the cell center are driven by multilayered transport mechanisms; that is, individual organelles can use kinesin-related proteins and myosins, as well as conventional kinesin, to move toward the cell periphery. In this case, other motors can compensate for the loss of conventional kinesin except in cells that have extremely long transport tracks.

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