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Related Concept Videos

Introduction to Membrane Traffic01:44

Introduction to Membrane Traffic

The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
Maturation of Endosomes01:28

Maturation of Endosomes

The early endosome containing internalized molecules matures through transformations in its location, morphology, intraluminal pH, and membrane protein composition. Together, these changes result in a more acidic late endosome that contains multiple intraluminal vesicles; therefore, the late endosome is also called a multivesicular body (MVB).
Changes in location
The maturing endosome moves along microtubules from the periphery of the cell towards the perinuclear region. This movement of the...
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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...
Separation of Sister Chromatids02:17

Separation of Sister Chromatids

At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
At the onset of anaphase, separase, a proteolytic enzyme, is...
Role of Septins01:02

Role of Septins

Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...

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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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Securin and separase modulate membrane traffic by affecting endosomal acidification.

Marina Bacac1, Carlo Fusco, Anne Planche

  • 1Division of Experimental Pathology, Faculty of Biology and Medicine, Institute of Pathology, CHUV, University of Lausanne, Rue du Bugnon 25, Lausanne CH1011, Switzerland.

Traffic (Copenhagen, Denmark)
|January 29, 2011
PubMed
Summary

Securin and separase regulate cell division but also impact membrane traffic. Depleting these proteins disrupts the Golgi and endosomes, affecting protein secretion and recycling.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • Securin and separase are known for their roles in sister chromatid separation during anaphase.
  • Emerging evidence suggests additional functions in membrane traffic in model organisms.

Purpose of the Study:

  • To investigate the role of securin and separase in membrane traffic and protein secretion in mammalian cells.
  • To elucidate the molecular mechanisms underlying these novel functions.

Main Methods:

  • Depletion of securin and separase using specific inhibitors or genetic techniques.
  • Microscopy to observe cellular structures like the trans-Golgi network (TGN) and endosomes.
  • Assays to measure protein secretion, receptor recycling, and endosome acidification.

Main Results:

  • Securin and separase associate with cellular membranes.
  • Depletion leads to trans-Golgi network swelling and enlarged endocytic vesicles.
  • Impaired constitutive protein secretion, receptor recycling, and degradation observed.
  • Defective early endosome acidification and increased vacuolar (V-) ATPase recruitment occurred.

Conclusions:

  • Securin and separase have a novel function in modulating membrane traffic and protein secretion in mammalian cells.
  • These proteins are involved in regulating the assembly and function of vacuolar (V-) ATPase complexes.
  • Findings reveal a new layer of complexity in the roles of securin and separase beyond chromosome segregation.