scholarly journals Kinesin light chain-independent function of the Kinesin heavy chain in cytoplasmic streaming and posterior localisation in the Drosophila oocyte

Development ◽  
2002 ◽  
Vol 129 (23) ◽  
pp. 5473-5485 ◽  
Author(s):  
I. M. Palacios
Keyword(s):  
Heavy Chain ◽  
Light Chain ◽  
Cytoplasmic Streaming ◽  
Independent Function ◽  
Kinesin Light Chain ◽  
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.

The C-Terminal Region of the Stalk Domain of Ubiquitous Human Kinesin Heavy Chain Contains the Binding Site for Kinesin Light Chain†

Biochemistry ◽  
1998 ◽  
Vol 37 (47) ◽  
pp. 16663-16670 ◽  
Author(s):  
Russell J. Diefenbach ◽  
Joel P. Mackay ◽  
Patricia J. Armati ◽  
Anthony L. Cunningham
Keyword(s):  
Binding Site ◽  
Heavy Chain ◽  
Light Chain ◽  
Terminal Region ◽  
Kinesin Light Chain ◽  
Kinesin Heavy Chain ◽  
Stalk Domain

scholarly journals Defective Kinesin Heavy Chain Behavior in Mouse Kinesin Light Chain Mutants

1999 ◽  
Vol 146 (6) ◽  
pp. 1277-1288 ◽  
Author(s):  
Amena Rahman ◽  
Adeela Kamal ◽  
Elizabeth A. Roberts ◽  
Lawrence S.B. Goldstein
Keyword(s):  
Heavy Chain ◽  
Light Chain ◽  
Mutant Mice ◽  
Kinesin Light Chain ◽  
Kinesin Heavy Chain ◽  
Neuronal Tissues ◽  
Biochemical Analyses ◽  
Conventional Kinesin

Conventional kinesin, kinesin-I, is a heterotetramer of two kinesin heavy chain (KHC) subunits (KIF5A, KIF5B, or KIF5C) and two kinesin light chain (KLC) subunits. While KHC contains the motor activity, the role of KLC remains unknown. It has been suggested that KLC is involved in either modulation of KHC activity or in cargo binding. Previously, we characterized KLC genes in mouse (Rahman, A., D.S. Friedman, and L.S. Goldstein. 1998. J. Biol. Chem. 273:15395–15403). Of the two characterized gene products, KLC1 was predominant in neuronal tissues, whereas KLC2 showed a more ubiquitous pattern of expression. To define the in vivo role of KLC, we generated KLC1 gene-targeted mice. Removal of functional KLC1 resulted in significantly smaller mutant mice that also exhibited pronounced motor disabilities. Biochemical analyses demonstrated that KLC1 mutant mice have a pool of KIF5A not associated with any known KLC subunit. Immunofluorescence studies of sensory and motor neuron cell bodies in KLC1 mutants revealed that KIF5A colocalized aberrantly with the peripheral cis-Golgi marker giantin in mutant cells. Striking changes and aberrant colocalization were also observed in the intracellular distribution of KIF5B and β′-COP, a component of COP1 coatomer. Taken together, these data best support models that suggest that KLC1 is essential for proper KHC activation or targeting.

LIPOPOLYSACCHARIDE-SENSITIVE SERINE-PROTEASE ZYMOGEN (FACTOR C) OF LIMULUS HEMOCYTES: IDENTIFICATION AND ALIGNMENT OF PROTEOLYTIC FRAGMENTS PRODUCED DURING THE ACTIVATION SHOW THAT IT IS A NOVEL TYPE OF SERINE-PROTEASE

1987 ◽  
Author(s):  
F Tokunaga ◽  
T Miyata ◽  
T Nakamura ◽  
T Morita ◽  
S Iwanaga
Keyword(s):  
Serine Protease ◽  
Heavy Chain ◽  
Light Chain ◽  
Interleukin 2 ◽  
Coagulation Factor ◽  
Clotting Factor ◽  
Single Chain ◽  
Terminal Sequence ◽  
A Chain ◽  
Factor C

Limulus clotting factor, factor C, is a lipopolysaccharide (LPS)-sensitive serine-protease zymogen present in the hemocytes. It is a two-chain glycoprotein (M.W. = 123,000) composed of a heavy chain (M.W. = 80,000) and a light chain (M.W. = 43,000) T. Nakamura et al. (1986) Eur. J. Biochem. 154, 511-521 .On further studies of this zymogen, a single-chain factor C (M.W. = 123,000) was identified by Western blotting technique. The heavy chain had an NH2-terminal sequence of Ser-Gly-Val-Asp-, which was consistent with the NH2-terminal sequence of the single-chain factor C, indicating that the heavy chain is located in the NH2-terminal part of the zymogen. The light chain had an NH22-terminal sequence of Ser-Ser-Gln-Pro-. Incubation of the two-chain zymogen with LPS resulted in the cleavage of a Phe-Ile bond between residues 72 and 73 of the light chain. Concomitant with this cleavage, the A (72.amino acids) and B chains derived from the light chain was formed. The complete amino acid sequence of the A chain was determined by automated Edman degradation. The A chain contained a typical segment which is similar structuraly to those a family of repeats in human β2 -glycoprotein I, complement factors B, Clr, Cls, H, C4b-binding protein, 02, coagulation factor XIII b subunit, haptoglobin a chain, and interleukin 2 receptor. The NH2-terminal sequence of the B chain was Ile-Trp-Asn-Gly-. This chain contained the serine-active site sequence of -ASP-Ala-Cys-Ser-Gly-Asp-SER-Gly-Gly-Pro-.These results indicate that limulus factor C exists in the hemocytes in a single-chain zymogen form and is converted to an active serine-protease by hydrolysis of a specific Phe-Ile peptide bond. The correlation of limulus factor C and mammalian complement proteins was also suggested.

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