scholarly journals Phosphorylation on threonine 11 of β-dystrobrevin alters its interaction with kinesin heavy chain

FEBS Journal ◽  
2012 ◽  
Vol 279 (22) ◽  
pp. 4131-4144 ◽  
Author(s):  
Federica Fratini ◽  
Gianfranco Macchia ◽  
Paola Torreri ◽  
Andrea Matteucci ◽  
Anna Maria Salzano ◽  
...  
Keyword(s):  
Heavy Chain ◽  
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 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.

The suppression of testis-brain RNA binding protein and kinesin heavy chain disrupts mRNA sorting in dendrites

1999 ◽  
Vol 112 (21) ◽  
pp. 3691-3702 ◽  
Author(s):  
W.L. Severt ◽  
T.U. Biber ◽  
X. Wu ◽  
N.B. Hecht ◽  
R.J. DeLorenzo ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Antisense Oligonucleotides ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Dependent Manner ◽  
Mobility Shift ◽  
Neuronal Remodeling ◽  
Kinesin Heavy Chain ◽  
Gel Mobility Shift

Ribonucleoprotein particles (RNPs) are thought to be key players in somato-dendritic sorting of mRNAs in CNS neurons and are implicated in activity-directed neuronal remodeling. Here, we use reporter constructs and gel mobility shift assays to show that the testis brain RNA-binding protein (TB-RBP) associates with mRNPs in a sequence (Y element) dependent manner. Using antisense oligonucleotides (anti-ODN), we demonstrate that blocking the TB-RBP Y element binding site disrupts and mis-localizes mRNPs containing (alpha)-calmodulin dependent kinase II (alpha)-CAMKII) and ligatin mRNAs. In addition, we show that suppression of kinesin heavy chain motor protein alters only the localization of (alpha)-CAMKII mRNA. Thus, differential sorting of mRNAs involves multiple mRNPs and selective motor proteins permitting localized mRNAs to utilize common mechanisms for shared steps.

scholarly journals Subunit Interactions in Dimeric Kinesin Heavy Chain Derivatives That Lack the Kinesin Rod

1995 ◽  
Vol 270 (8) ◽  
pp. 3926-3931 ◽  
Author(s):  
Edgar C. Young ◽  
Elise Berliner ◽  
Hansraj K. Mahtani ◽  
Bernardo Perez-Ramirez ◽  
Jeff Gelles
Keyword(s):  
Heavy Chain ◽  
Subunit Interactions ◽  
Kinesin Heavy Chain

The C. elegans unc-104 4 gene encodes a putative kinesin heavy chain-like protein

Neuron ◽  
1991 ◽  
Vol 6 (1) ◽  
pp. 113-122 ◽  
Author(s):  
Anthony J. Otsuka ◽  
Ayyamperumal Jeyaprakash ◽  
Jaime García-Añoveros ◽  
Lan Zhao Tang ◽  
Gregory Fisk ◽  
...  
Keyword(s):  
Heavy Chain ◽  
C Elegans ◽  
Kinesin Heavy Chain

scholarly journals Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent

2006 ◽  
Vol 173 (4) ◽  
pp. 545-557 ◽  
Author(s):  
Elizabeth E. Glater ◽  
Laura J. Megeath ◽  
R. Steven Stowers ◽  
Thomas L. Schwarz
Keyword(s):  
Heavy Chain ◽  
Light Chain ◽  
Adaptor Protein ◽  
Direct Interaction ◽  
Anterograde Transport ◽  
Kinesin Light Chain ◽  
Energy Demands ◽  
Kinesin Heavy Chain ◽  
Conventional Kinesin ◽  
Dependent Transport

Mitochondria are distributed within cells to match local energy demands. We report that the microtubule-dependent transport of mitochondria depends on the ability of milton to act as an adaptor protein that can recruit the heavy chain of conventional kinesin-1 (kinesin heavy chain [KHC]) to mitochondria. Biochemical and genetic evidence demonstrate that kinesin recruitment and mitochondrial transport are independent of kinesin light chain (KLC); KLC antagonizes milton's association with KHC and is absent from milton–KHC complexes, and mitochondria are present in klc −/− photoreceptor axons. The recruitment of KHC to mitochondria is, in part, determined by the NH2 terminus–splicing variant of milton. A direct interaction occurs between milton and miro, which is a mitochondrial Rho-like GTPase, and this interaction can influence the recruitment of milton to mitochondria. Thus, milton and miro are likely to form an essential protein complex that links KHC to mitochondria for light chain–independent, anterograde transport of mitochondria.

Sign in / Sign up

Export Citation Format

Share Document