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

The Early Endosome: Endocytosis of Transferrin01:28

The Early Endosome: Endocytosis of Transferrin

Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
Recycling Endosomes and Transcytosis00:58

Recycling Endosomes and Transcytosis

The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
The recycling endosome is not a single organelle but an extensively tubulated network of recycling pathways. It functions in storing molecules or transporting them across...
ER Retrieval Pathway01:45

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

You might also read

Related Articles

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

Sort by
Same author

Substantial and sustained reduction in under-5 mortality, diarrhea, and pneumonia in Oshikhandass, Pakistan: evidence from two longitudinal cohort studies 15 years apart.

BMC public health·2020
Same author

Tamoxifen Acts as a Parietal Cell Protonophore.

Cellular and molecular gastroenterology and hepatology·2020
Same author

A meta-analysis of the accuracy of a neuroendocrine tumor mRNA genomic biomarker (NETest) in blood.

Annals of oncology : official journal of the European Society for Medical Oncology·2020
Same author

Corrigendum to "Identification of a CIP4 PKA phosphorylation site involved in the regulation of cancer cell invasiveness and metastasis" [Canc. Lett. 461 (2019) 65-77].

Cancer letters·2020
Same author

Rab25 as a tumour suppressor in colon carcinogenesis.

British journal of cancer·2010
Same author

Brefeldin A rapidly disrupts plasma membrane polarity by blocking polar sorting in common endosomes of MDCK cells.

Journal of cell science·2001

Related Experiment Video

Updated: Jul 14, 2026

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins
09:22

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins

Published on: December 13, 2013

Rab11 is associated with transferrin-containing recycling compartments in K562 cells

E G Green1, E Ramm, N M Riley

  • 1Department of Nutrition, Harvard School of Public Health, Boston, Massachusetts 02115, USA.

Biochemical and Biophysical Research Communications
|November 5, 1997
PubMed
Summary

Researchers identified Rab11, a GTP-binding protein, in K562 cells using 3'RACE PCR. This finding suggests Rab11 may have a role in protein trafficking and recycling within non-polarized cells.

More Related Videos

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis
07:54

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Published on: August 22, 2018

Density Gradient Ultracentrifugation for Investigating Endocytic Recycling in Mammalian Cells
05:13

Density Gradient Ultracentrifugation for Investigating Endocytic Recycling in Mammalian Cells

Published on: June 30, 2021

Related Experiment Videos

Last Updated: Jul 14, 2026

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins
09:22

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins

Published on: December 13, 2013

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis
07:54

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Published on: August 22, 2018

Density Gradient Ultracentrifugation for Investigating Endocytic Recycling in Mammalian Cells
05:13

Density Gradient Ultracentrifugation for Investigating Endocytic Recycling in Mammalian Cells

Published on: June 30, 2021

Area of Science:

  • Cell biology
  • Molecular biology
  • Protein trafficking

Background:

  • Rab GTPases are key regulators of intracellular membrane trafficking.
  • Rab11 is typically associated with polarized and secretory cells.
  • The K562 cell line is a human hematopoietic cell line often used in cancer research.

Purpose of the Study:

  • To investigate Rab transcript expression in the K562 cell line.
  • To identify novel Rab proteins in non-polarized hematopoietic cells.
  • To understand the potential function of Rab11 in non-polarized cell contexts.

Main Methods:

  • 3'RACE PCR was employed to survey Rab transcripts.
  • Quantitative analysis of Rab mRNA and protein levels was performed.
  • Confocal immunofluorescence microscopy was utilized for protein localization studies.

Main Results:

  • Rab11 was identified as a GTP-binding protein in K562 cells.
  • Rab11 mRNA was found to be abundant in K562 cells.
  • Rab11 protein localized with transferrin in recycling/exocytic compartments.

Conclusions:

  • The presence of Rab11 in non-polarized K562 cells challenges previous assumptions about its cellular distribution.
  • Rab11 may play a role in the trafficking and recycling of internalized proteins in non-polarized and non-secretory cells.
  • Further investigation into Rab11 function in diverse cell types is warranted.