Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

MAPK Signaling Cascades01:07

MAPK Signaling Cascades

6.4K
Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
6.4K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

4.1K
The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
4.1K
M-Cdk Drives Transition Into Mitosis02:15

M-Cdk Drives Transition Into Mitosis

5.7K
Checkpoints throughout the cell cycle serve as safeguards and gatekeepers, allowing the cell cycle to progress in favorable conditions and slow or halt it in problematic ones. This regulation is known as the cell cycle control system.
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...
5.7K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

7.3K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
7.3K
Regulated Protein Degradation02:58

Regulated Protein Degradation

7.8K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
7.8K
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

3.9K
The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
3.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

GloBIAS: strengthening the foundations of bioimage analysis.

Nature methods·2026
Same author

Interaction of HS1BP3 with cortactin modulates TKS5 localisation, cell secretion and cancer malignancy.

Molecular oncology·2026
Same author

LRRC59 cooperates with nuclear transporters to restrain the nuclear envelope repair machinery and safeguard genome integrity.

Nature communications·2025
Same author

The RAB27A effector SYTL5 regulates mitophagy and mitochondrial metabolism.

eLife·2025
Same author

A chaperone-proteasome-based fragmentation machinery is essential for aggrephagy.

Nature cell biology·2025
Same author

SNX10 at the crossroad of endocytosis and piecemeal mitophagy.

Autophagy·2025

Related Experiment Video

Updated: Oct 7, 2025

Time-Lapse Video Microscopy for Assessment of EYFP-Parkin Aggregation as a Marker for Cellular Mitophagy
09:29

Time-Lapse Video Microscopy for Assessment of EYFP-Parkin Aggregation as a Marker for Cellular Mitophagy

Published on: May 4, 2016

7.3K

GAK and PRKCD kinases regulate basal mitophagy.

Michael J Munson1,2,3, Benan J Mathai1,2, Matthew Yoke Wui Ng1,2

  • 1Division of Biochemistry, Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.

Autophagy
|January 10, 2022
PubMed
Summary

This study identifies two kinases, GAK and PRKCD, as key regulators of basal mitophagy, a crucial cellular housekeeping process. Their findings reveal new mechanisms controlling mitochondrial quality control independent of PRKN.

Keywords:
Cyclin-G-associated kinaseGAKPKCPRKCDPRKNmitophagyprotein kinase C

More Related Videos

In Vitro and In Vivo Detection of Mitophagy in Human Cells, C. Elegans, and Mice
08:40

In Vitro and In Vivo Detection of Mitophagy in Human Cells, C. Elegans, and Mice

Published on: November 22, 2017

17.8K
Visualization of Endogenous Mitophagy Complexes In Situ in Human Pancreatic Beta Cells Utilizing Proximity Ligation Assay
08:40

Visualization of Endogenous Mitophagy Complexes In Situ in Human Pancreatic Beta Cells Utilizing Proximity Ligation Assay

Published on: May 2, 2019

6.0K

Related Experiment Videos

Last Updated: Oct 7, 2025

Time-Lapse Video Microscopy for Assessment of EYFP-Parkin Aggregation as a Marker for Cellular Mitophagy
09:29

Time-Lapse Video Microscopy for Assessment of EYFP-Parkin Aggregation as a Marker for Cellular Mitophagy

Published on: May 4, 2016

7.3K
In Vitro and In Vivo Detection of Mitophagy in Human Cells, C. Elegans, and Mice
08:40

In Vitro and In Vivo Detection of Mitophagy in Human Cells, C. Elegans, and Mice

Published on: November 22, 2017

17.8K
Visualization of Endogenous Mitophagy Complexes In Situ in Human Pancreatic Beta Cells Utilizing Proximity Ligation Assay
08:40

Visualization of Endogenous Mitophagy Complexes In Situ in Human Pancreatic Beta Cells Utilizing Proximity Ligation Assay

Published on: May 2, 2019

6.0K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • Cellular homeostasis relies on programmed removal of mitochondria (mitophagy).
  • While stress-induced mitophagy (often PRKN-dependent) is well-studied, basal mitophagy mechanisms remain less understood.
  • Investigating PRKN-independent mitophagy is crucial for a complete understanding of mitochondrial quality control.

Purpose of the Study:

  • To identify novel regulators of basal, PRKN-independent mitophagy.
  • To elucidate the molecular mechanisms by which these regulators control mitophagy.
  • To validate the in vivo relevance of identified mitophagy regulators.

Main Methods:

  • Utilized siRNA screening of lipid-binding proteins to identify regulators of PRKN-independent mitophagy induced by iron chelation (deferiprone).
  • Investigated the localization and function of identified kinases (GAK, PRKCD) using cell-based assays.
  • Assessed the impact of kinase impairment on mitophagy and mitochondrial/lysosomal morphology in vivo.

Main Results:

  • Identified GAK (cyclin G associated kinase) and PRKCD (protein kinase C delta) as positive regulators of PRKN-independent mitophagy.
  • Demonstrated PRKCD's role in recruiting ULK1-ATG13 to mitochondria during mitophagy induction.
  • Showed GAK's involvement in altering mitochondrial network and lysosomal morphology, impacting mitochondrial transport for degradation.
  • Confirmed that impairing either GAK or PRKCD in vivo blocks basal mitophagy.

Conclusions:

  • GAK and PRKCD are critical regulators of basal mitophagy, operating independently of PRKN.
  • PRKCD and GAK employ distinct mechanisms to control mitophagy initiation and execution.
  • These findings highlight novel therapeutic targets for diseases associated with mitochondrial dysfunction.