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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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2014-12, Vol.78 (12), p.2069-2072
Hauptverfasser:	Jang, Won Hee, Jeong, Young Joo, Choi, Sun Hee, Kim, Sang-Jin, Urm, Sang-Hwa, Seog, Dae-Hyun
Format:	Artikel
Sprache:	eng
Schlagworte:	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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Zusammenfassung:	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