Endoplasmic reticulum

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27 Terms

1
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What is the central role of the endoplasmic reticulum (rough and smooth) ?

Lipid and protein biosynthesis

2
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What ER consists of (structure) ?

  • ER membrane : continuous with the nuclear envelope

  • ER lumen : 10% of the total volume

3
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What are the two types of ER ?

  • Smooth ER : no ribosome

  • Rough ER : ribosomes on the outer surface

4
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What are the functions of rough ER ?

  • protein folding and assembly

  • post-translational protein modification

  • protein transport

  • membrane protein production

5
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What are ribosomes made of ?

RNA (rRNA) and protein

6
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Are ribosomes membrane organelles ?

NO, they lack a surrounding membrane

7
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Where do ribosomes bind ?

  • Nuclear envelope

  • Rough ER

8
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Where are located ribosomes ?

  • Cytoplasm : free ribosomes

  • RER (cytosolic side) and Nuclear envelope : membrane-bound ribosomes

  • Mitochondria

  • Chloroplasts

9
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Where are initially located all ribosomes ?

There is a common pool of free ribosomes in the cytoplasm, then they are orienting themselves thanks to signal sequence

10
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What is the future location of a protein synthesised in free ribosomes ?

  • Remain in the cytosol

  • Nucleus

  • Mitochondria

  • Chloroplasts

  • Peroxisome

<ul><li><p>Remain in the cytosol</p></li><li><p>Nucleus</p></li><li><p>Mitochondria</p></li><li><p>Chloroplasts</p></li><li><p>Peroxisome</p></li></ul><p></p>
11
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What is the future location of a protein synthesised in membrane-bound ribosomes ?

  • lumen of ER —> Golgi apparatus

  • Lysosomes

  • Secretory vesicles (cell exterior)

  • Plasma membrane

<ul><li><p>lumen of ER —&gt; Golgi apparatus</p></li><li><p>Lysosomes</p></li><li><p>Secretory vesicles (cell exterior)</p></li><li><p>Plasma membrane</p></li></ul><p></p>
12
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Where are assembled ribosomal subunits ?

Directly into the nucleolus by the association of newly transcribed and modified rRNAs with ribosomal proteins

13
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Between eukaryotic and prokaryotic ribosomes, which one is the biggest ?

Eukaryotic ribosome (80S) > Prokaryotic ribosome (70S)

14
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When does ER protein translocation occur ?

Before the polypeptide chain is completely synthesised = co-translational translocation

15
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How does ER signal sequence is guided to the ER membrane ?

With the help of two components :

  • Signal-Recognition Particle (SRP) : binds to the signal sequence

  • SRP receptor : in the RER membrane

<p>With the help of two components : </p><ul><li><p>Signal-Recognition Particle (SRP) : binds to the signal sequence</p></li><li><p>SRP receptor : in the RER membrane</p></li></ul><p></p>
16
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What causes signal recognition particle (SRP) binding on ER signal sequence ?

Because of a ‘pause’ in the protein synthesis

17
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What is the structure that cleaves the signal sequence from the final translocated protein ?

Signal peptidase, which allows the hydrophobic signal sequence to diffuses through the bilayer, where it is degraded into AA by proteases in the ER

<p><strong><u>Signal peptidase</u></strong>, which allows the hydrophobic signal sequence to diffuses through the bilayer, where it is degraded into AA by proteases in the ER</p>
18
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What is the difference between single and multiples transmembrane proteins ?

  • Single pass transmembrane protein : contains either a stop-transfer sequence or an internal signal sequence that is not cleaved off

  • Multipass transmembrane protein : contains both stop-transfer sequence and internal signal sequence and have several of these

<ul><li><p>Single pass transmembrane protein : contains either a stop-transfer sequence or an internal signal sequence that is not cleaved off</p></li><li><p>Multipass transmembrane protein : contains both stop-transfer sequence and internal signal sequence and have several of these</p></li></ul><p></p>
19
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<p>Describe this situation</p>

Describe this situation

This is an EXCEPTION where a protein is fully translocated through a free ribosome and is being transported through the help of chaperones that help the protein not folding, and reach the ER membrane where their signal sequence will be recognised by a complex protein associated with the translocation channel in the ER membrane, named a BiP (type of chaperone)

20
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What is the purpose of BiP chaperones ?

they mediate protein folding and the assembly of multi subunit proteins

21
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What happens to protein that fail to achieve their properly fold in the ER ?

They leave the ER lumen through the same translocator where they came from, and goes into the cytosol to be degraded into the proteasome

<p>They leave the ER lumen through the same translocator where they came from, and goes into the cytosol to be degraded into the <strong><u>proteasome</u></strong></p>
22
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On what type of AA, polypeptide chain, is being glycosylated ?

Asparagine

<p>Asparagine</p>
23
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What are the functions of the smooth ER ?

  • Lipid metabolism : lipids and lipoprotein synthesis

  • Detoxification process : drugs & harmful compounds produced by metabolism

  • Calcium storage : sequester Ca2+ from the cytosol

24
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In what kind of cells smooth ER is abundant ?

In cells specialised in synthesis of steroid hormones form cholesterol (liver cells, adrenal cells, gonadal cells)

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What kind of cell is the principal site of production of lipoproteins ?

Hepatocytes in the liver

26
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In the hepatocytes, where are synthesised lipoproteins ?

in the SER

27
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What type of ER is sarcoplasmic reticulum ?

Smooth Endoplasmic Reticulum