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Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

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Overview
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Endocytosis01:16

Endocytosis

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Eukaryotic cells acquire nutrients for growth and proliferation. Nutrients and other molecules that require degradation are internalized from the extracellular space by a process called endocytosis. The term ‘endocytosis' was first coined by Christian de Duve in 1963.
Endocytosis always begins with the plasma membrane enclosing an incoming molecule to form a transport vesicle which, in some cases, can be coated with a protein called ‘clathrin.' Endocytosed material is either...
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Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

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Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
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Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
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Exocrine Glands: Methods of Secretion01:08

Exocrine Glands: Methods of Secretion

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Exocrine glands are those that release their secretions through ducts. Based on their mode of secretion, they can be classified into merocrine, apocrine, and holocrine.
Merocrine Secretion
Merocrine secretion is the most common type of exocrine secretion. The secretions are enclosed in vesicles and moved to the cell's apical surface, where the contents are released by exocytosis. For example, mucous, a watery secretion rich in the glycoprotein mucin, is a merocrine secretion. The eccrine...
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Drug Elimination by Renal Route: Tubular Secretion01:15

Drug Elimination by Renal Route: Tubular Secretion

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Once the process of glomerular filtration is completed, blood carrying unfiltered drug molecules traverses through efferent arterioles and makes its way into the peritubular capillaries in the proximal tubule. A variety of carriers play a pivotal role in actively secreting drugs from these peritubular capillaries into the tubular fluid. The organic anion transporter transfers acidic drugs, against an electrochemical gradient, from the peritubular capillaries into the renal tubule cells and...
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Related Experiment Video

Updated: May 6, 2026

Glycopeptide Capture for Cell Surface Proteomics
10:11

Glycopeptide Capture for Cell Surface Proteomics

Published on: May 10, 2014

11.0K

GRASPing unconventional secretion.

Stephanie K Levi1, Benjamin S Glick

  • 1Department of Molecular Genetics and Cell Biology, The University of Chicago, 920 East 58th Street, Chicago, IL 60637, USA.

Cell
|August 19, 2007
PubMed
Summary

GRASP proteins, involved in Golgi apparatus functions, are surprisingly essential for an unconventional secretory pathway. This pathway bypasses the standard Golgi-dependent membrane traffic route, revealing novel cellular transport mechanisms.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Function

Background:

  • GRASP proteins are known to associate with the Golgi apparatus.
  • They have been implicated in Golgi cisternae stacking, vesicle tethering, and mitotic progression.
  • However, their precise functions remain largely undefined.

Purpose of the Study:

  • To investigate the specific roles of GRASP proteins in cellular processes.
  • To elucidate the function of a GRASP homolog in membrane traffic.
  • To identify novel secretory pathways involving GRASP proteins.

Main Methods:

  • Utilized a GRASP homolog in experimental models.
  • Investigated membrane traffic pathways.
  • Analyzed Golgi-dependent and independent routes.

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Hydrogel Nanoparticle Harvesting of Plasma or Urine for Detecting Low Abundance Proteins
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Hydrogel Nanoparticle Harvesting of Plasma or Urine for Detecting Low Abundance Proteins

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Last Updated: May 6, 2026

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Glycopeptide Capture for Cell Surface Proteomics

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Capture Compound Mass Spectrometry - A Powerful Tool to Identify Novel c-di-GMP Effector Proteins
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Capture Compound Mass Spectrometry - A Powerful Tool to Identify Novel c-di-GMP Effector Proteins

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Hydrogel Nanoparticle Harvesting of Plasma or Urine for Detecting Low Abundance Proteins
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Hydrogel Nanoparticle Harvesting of Plasma or Urine for Detecting Low Abundance Proteins

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Main Results:

  • A GRASP homolog was found to be unexpectedly required for a specific secretory pathway.
  • This pathway represents an unconventional route for membrane transport.
  • The identified pathway bypasses the conventional Golgi-dependent route.

Conclusions:

  • GRASP proteins play a critical, previously unrecognized role in unconventional secretion.
  • This finding expands our understanding of Golgi-independent membrane trafficking.
  • The study highlights a novel mechanism for cellular transport bypassing standard Golgi pathways.