Dynamin-1-like protein (Dnm1L) interaction with kinesin light chain 1 (KLC1) through the tetratricopeptide repeat (TPR) domains

Kinesin light chain 1 (KLC1) mediates binding of KIF5 motor to specific cargo. Using the yeast two-hybrid screening, we found that mitochondrial fission protein dynamin-1-like protein (Dnm1L) interacted with KLC1, but not KIF5. Dnm1L and KLC1 were co-localized in cultured cells. These results sugges...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2014-12, Vol.78 (12), p.2069-2072
Main Authors: Jang, Won Hee, Jeong, Young Joo, Choi, Sun Hee, Kim, Sang-Jin, Urm, Sang-Hwa, Seog, Dae-Hyun
Format: Article
Language:English
Subjects:
Binding Sites
Biological Transport
Dnm1L
Gene Expression Regulation
GTP Phosphohydrolases - genetics
GTP Phosphohydrolases - metabolism
HEK293 Cells
Humans
Kinesin - genetics
Kinesin - metabolism
kinesin 1
KLC1
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Mitochondria - genetics
Mitochondria - metabolism
Mitochondrial Dynamics - genetics
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
Protein Binding
Protein Structure, Tertiary
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Signal Transduction
TPR domain
Two-Hybrid System Techniques
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Summary:Kinesin light chain 1 (KLC1) mediates binding of KIF5 motor to specific cargo. Using the yeast two-hybrid screening, we found that mitochondrial fission protein dynamin-1-like protein (Dnm1L) interacted with KLC1, but not KIF5. Dnm1L and KLC1 were co-localized in cultured cells. These results suggest that KLC1 may play a potential role in post-fission mitochondrial transport.
ISSN:0916-8451
1347-6947
DOI:10.1080/09168451.2014.943652