Related Experiment Video

Updated: Apr 26, 2026

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy
08:06

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Published on: February 14, 2016

11.2K

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

Won Hee Jang1, Young Joo Jeong, Sun Hee Choi

  • 1a Department of Biochemistry and u-HARC , Inje University College of Medicine , Busan , Korea.

Bioscience, Biotechnology, and Biochemistry
|August 2, 2014
PubMed

Insights

Mitochondrial fission protein dynamin-1-like protein (Dnm1L) interacts with kinesin light chain 1 (KLC1), suggesting KLC1

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Neuroscience

Background:

  • Kinesin light chain 1 (KLC1) is crucial for KIF5 motor-mediated cargo binding.
  • Mitochondrial dynamics, including fission and transport, are vital for cellular function.

Purpose of the Study:

  • To investigate the interaction between mitochondrial fission protein dynamin-1-like protein (Dnm1L) and KLC1.
  • To explore the potential role of KLC1 in post-fission mitochondrial transport.

Main Methods:

  • Yeast two-hybrid screening to identify protein interactions.
  • Co-localization studies in cultured cells.

Main Results:

  • Dynamin-1-like protein (Dnm1L) was found to interact with kinesin light chain 1 (KLC1).
  • This interaction was specific to KLC1 and did not involve KIF5.
  • Dnm1L and KLC1 were observed to co-localize within cultured cells.

Conclusions:

  • Kinesin light chain 1 (KLC1) may function in the transport of mitochondria after fission.
  • The interaction between Dnm1L and KLC1 suggests a novel regulatory mechanism in mitochondrial dynamics.
Keywords:
Dnm1LKLC1TPR domainkinesin 1

More Related Videos

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis11:09

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis

Published on: October 30, 2014

9.2K
Directly Measuring Forces Within Reconstituted Active Microtubule Bundles07:47

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Published on: May 10, 2022

1.4K

Related Concept Videos

Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular...
10.0K
The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
5.4K
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
2.9K
Anaphase A and B01:39

Anaphase A and B

Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
4.3K
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
3.1K
Nuclear Export01:42

Nuclear Export

The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
3.7K