Moving Proteins into Membranes &

Organelles
Associated Readings: Ch.13
Chapter 13 – Moving Proteins into Membranes
and Organelles
Chapter 13 – Moving Proteins into Membranes
and Organelles
13.1 Targeting Proteins To and Across the ER
Membrane
13.2 Insertion of Membrane Proteins into the ER
13.3 Protein Modifications, Folding, and Quality
Control in the ER
13.4 Targeting of Proteins to Mitochondria and
Chloroplasts
13.5 Targeting of Peroxisomal Proteins
13.6 Transport Into and Out of the Nucleus
Chapter 13 – Moving Proteins into Membranes
and Organelles
13.1 Targeting Proteins To and Across the ER
Membrane
13.2 Insertion of Membrane Proteins into the ER
13.3 Protein Modifications, Folding, and Quality
Control in the ER
13.4 Targeting of Proteins to Mitochondria and
Chloroplasts
13.5 Targeting of Peroxisomal Proteins
13.6 Transport Into and Out of the Nucleus
Targeting Proteins To and Across
the ER Membrane
1. Overview of major
protein-sorting
pathways in eukaryotes
2. Cotranslational
translocation
3. Post-translational
translocation
Targeting Proteins To and Across
the ER Membrane
1. Overview of major
protein-sorting
pathways in eukaryotes
2. Cotranslational
translocation
3. Post-translational
translocation
Targeting Proteins To and Across
the ER Membrane

https://www.3dmoleculardesigns.com/Teacher-Resources/
1. Overview of major

Amino-Acid-Starter-Kit/Teacher-Notes.htm
protein-sorting
pathways in eukaryotes
2. Cotranslational
translocation
3. Post-translational
translocation

“beginning” “tail end”

Targeting Proteins To and Across
the ER Membrane
1. Overview of major
protein-sorting
pathways in eukaryotes
2. Cotranslational
translocation
3. Post-translational
translocation
Targeting Proteins To and Across
the ER Membrane
1. Overview of major
protein-sorting
pathways in eukaryotes
2. Cotranslational
translocation
3. Post-translational
translocation
Targeting Proteins To and Across
the ER Membrane
1. Overview of major
protein-sorting
pathways in eukaryotes
2. Cotranslational
translocation
3. Post-translational
translocation
Targeting Proteins To and Across
the ER Membrane
1. Overview of major
protein-sorting
pathways in eukaryotes
2. Cotranslational
translocation
3. Post-translational
translocation
Targeting Proteins To and Across
the ER Membrane
1. Overview of major
protein-sorting
pathways in eukaryotes
2. Cotranslational
translocation
3. Post-translational
translocation
Chapter 13 – Moving Proteins into Membranes
and Organelles
13.1 Targeting Proteins To and Across the ER
Membrane
13.2 Insertion of Membrane Proteins into the ER
13.3 Protein Modifications, Folding, and Quality
Control in the ER
13.4 Targeting of Proteins to Mitochondria and
Chloroplasts
13.5 Targeting of Peroxisomal Proteins
13.6 Transport Into and Out of the Nucleus
Insertion of Membrane Proteins
into the ER
1. Classes of ER membrane
proteins
2. Predicting membrane
protein topology
Insertion of Membrane Proteins
into the ER
1. Classes of ER membrane
proteins
2. Predicting membrane
protein topology
Insertion of Membrane Proteins
into the ER
1. Classes of ER membrane
proteins Type I single-pass
2. Predicting membrane transmembrane proteins
protein topology
Insertion of Membrane Proteins
into the ER
1. Classes of ER membrane
proteins Type II and Type III single-pass
2. Predicting membrane transmembrane proteins
protein topology
Insertion of Membrane Proteins
into the ER
1. Classes of ER membrane Tail-anchored proteins
proteins
2. Predicting membrane
protein topology
Insertion of Membrane Proteins
into the ER
1. Classes of ER membrane
proteins
2. Predicting membrane GPI-anchored proteins
protein topology
Insertion of Membrane Proteins
into the ER
1. Classes of ER membrane
proteins
2. Predicting membrane
protein topology
Chapter 13 – Moving Proteins into Membranes
and Organelles
13.1 Targeting Proteins To and Across the ER
Membrane
13.2 Insertion of Membrane Proteins into the ER
13.3 Protein Modifications, Folding, and Quality
Control in the ER
13.4 Targeting of Proteins to Mitochondria and
Chloroplasts
13.5 Targeting of Peroxisomal Proteins
13.6 Transport Into and Out of the Nucleus
 Protein Modifications, Folding,
and Quality Control in the ER
1. Protein modification by ER enzymes
2. ER chaperones and lectins ensure proper
protein folding
3. Transport of unassembled/misfolded
proteins back to the cytosol, where they
are degraded in the ubiquitin-proteasome
pathway
4. Transport of properly folded proteins
and assembled subunits from the rough ER
to the Golgi complex in vesicles
 Protein Modifications, Folding,
and Quality Control in the ER
1. Protein modification by ER enzymes
2. ER chaperones and lectins ensure proper
protein folding
3. Transport of unassembled/misfolded
proteins back to the cytosol, where they
are degraded in the ubiquitin-proteasome
pathway
4. Transport of properly folded proteins
and assembled subunits from the rough ER
to the Golgi complex in vesicles
• Oligosaccharide chains
promote protein folding,
stability, adhesion, and
recognition.
• Protein disulfide isomerase
(PDI) forms and rearranges
protein cysteine disulfide bonds
until the protein is folded into
the thermodynamically most
stable conformation.
• Peptidyl-prolyl isomerase
(PPI) accelerates rotation about
peptidyl-prolyl bonds in
unfolded segments of a
polypeptide. Prolyl
isomerizations can be the rate-
limiting step in the folding of
protein domains.
 Protein Modifications, Folding,
and Quality Control in the ER
1. Protein modification by ER enzymes
2. ER chaperones and lectins ensure proper
protein folding
3. Transport of unassembled/misfolded
proteins back to the cytosol, where they
are degraded in the ubiquitin-proteasome
pathway
4. Transport of properly folded proteins
and assembled subunits from the rough ER
to the Golgi complex in vesicles
 Protein Modifications, Folding,
and Quality Control in the ER
1. Protein modification by ER enzymes
2. ER chaperones and lectins ensure proper
protein folding
3. Transport of unassembled/misfolded
proteins back to the cytosol, where they
are degraded in the ubiquitin-proteasome
pathway
4. Transport of properly folded proteins
and assembled subunits from the rough ER
to the Golgi complex in vesicles
• Modifications of N-linked
oligosaccharides are used
to monitor folding and for
quality control.
• Dislocation: Misfolded
secretory proteins –
recognized by specific ER
membrane proteins and
targeted for transport from
the ER lumen into the
cytosol for degradation
 Protein Modifications, Folding,
and Quality Control in the ER
1. Protein modification by ER enzymes
2. ER chaperones and lectins ensure proper
protein folding
3. Transport of unassembled/misfolded
proteins back to the cytosol, where they
are degraded in the ubiquitin-proteasome
pathway
4. Transport of properly folded proteins
and assembled subunits from the rough ER
to the Golgi complex in vesicles
Chapter 13 – Moving Proteins into Membranes
and Organelles
13.1 Targeting Proteins To and Across the ER
Membrane
13.2 Insertion of Membrane Proteins into the ER
13.3 Protein Modifications, Folding, and Quality
Control in the ER
13.4 Targeting of Proteins to Mitochondria and
Chloroplasts
13.5 Targeting of Peroxisomal Proteins
13.6 Transport Into and Out of the Nucleus
 Targeting of Proteins to
Mitochondria and Chloroplasts
1. Targeting sequences
direct proteins from the
cytosol to organelles
2. Protein import into
mitochondria
3. Protein import into
chloroplasts
 Targeting of Proteins to
Mitochondria and Chloroplasts
1. Targeting sequences
direct proteins from the
cytosol to organelles
2. Protein import into
mitochondria
3. Protein import into
chloroplasts
 Targeting of Proteins to
Mitochondria and Chloroplasts
1. Targeting sequences
direct proteins from the
cytosol to organelles
2. Protein import into
mitochondria
3. Protein import into
chloroplasts

targeting sequences in
imported mitochondrial
proteins
 Targeting of Proteins to
Mitochondria and Chloroplasts
1. Targeting sequences
direct proteins from the
cytosol to organelles
2. Protein import into
mitochondria
3. Protein import into
chloroplasts

protein import into the

mitochondrial matrix
 Targeting of Proteins to
Mitochondria and Chloroplasts
1. Targeting sequences
direct proteins from the
cytosol to organelles
2. Protein import into
mitochondria
3. Protein import into
chloroplasts

pathways to the inner

mitochondrial
membrane from the
cytosol
 Targeting of Proteins to
Mitochondria and Chloroplasts
1. Targeting sequences
direct proteins from the
cytosol to organelles
2. Protein import into
mitochondria
3. Protein import into
chloroplasts

pathways to the
mitochondrial
intermembrane
space
 Targeting of Proteins to
Mitochondria and Chloroplasts
1. Targeting sequences
direct proteins from the
cytosol to organelles
2. Protein import into
mitochondria
3. Protein import into
chloroplasts
Chapter 13 – Moving Proteins into Membranes
and Organelles
13.1 Targeting Proteins To and Across the ER
Membrane
13.2 Insertion of Membrane Proteins into the ER
13.3 Protein Modifications, Folding, and Quality
Control in the ER
13.4 Targeting of Proteins to Mitochondria and
Chloroplasts
13.5 Targeting of Peroxisomal Proteins
13.6 Transport Into and Out of the Nucleus
Targeting of Peroxisomal Proteins
1. Import of peroxisomal
matrix proteins
2. Model of peroxisomal
biogenesis and division
Targeting of Peroxisomal Proteins
1. Import of peroxisomal
matrix proteins
2. Model of peroxisomal
biogenesis and division
Targeting of Peroxisomal Proteins
1. Import of peroxisomal
matrix proteins
2. Model of peroxisomal
biogenesis and division
Chapter 13 – Moving Proteins into Membranes
and Organelles
13.1 Targeting Proteins To and Across the ER
Membrane
13.2 Insertion of Membrane Proteins into the ER
13.3 Protein Modifications, Folding, and Quality
Control in the ER
13.4 Targeting of Proteins to Mitochondria and
Chloroplasts
13.5 Targeting of Peroxisomal Proteins
13.6 Transport Into and Out of the Nucleus
Transport Into and Out of
the Nucleus
1. Nuclear import of
proteins
2. Ran-dependent and Ran-
independent nuclear export
Transport Into and Out of
the Nucleus
1. Nuclear import of
proteins
2. Ran-dependent and Ran-
independent nuclear export
Transport Into and Out of
the Nucleus
1. Nuclear import of
proteins
2. Ran-dependent and Ran-
independent nuclear export
Explain mechanisms by which proteins
“know” where in the cell to go.