Chapter 12 Summary

Each organelle of a eukaryotic cell has its own characteristic set of

enzymes and other specialized molecules, and complex distribution
systems transport specific products from one compartment to
another.
Proteins can act as organelle-specific surface markers that direct
new deliveries of proteins and lipids to the appropriate organelle.
Cytosol: space of the cytoplasm outside the membrane-enclosed
organelles.
Many vital biochemical processes take place in membranes or on
their surfaces. Membrane-bound enzymes catalyze lipid
metabolism, and oxidative phosphorylation and photosynthesis both
require a membrane to couple the transport of H= to the synthesis of
ATP.
The cytoplasm is the
main site of protein
synthesis and
degradation, and
performs most of the
cells intermediary
metabolism it
degrades small
molecules and
synthesizes others to
provide the building
blocks of
macromolecules.

The

they
the
for
many
the

rough ER has many

ribosomes (have no
membranes) bound to its
cytosolic surface. Proteins are
transported into the ER as
are synthetized. The ER also
produces most of the lipid for
cell and functions as a store
Ca2+ ions. Regions of the ER
without ribosomes are the
smooth ER. The ER sends
of its proteins and lipids to
Golgi apparatus, which
dispatches them to various
destinations.

Lysosomes contain digestive enzymes that degrade defunct

intracellular organelles, as well as macromolecules and particles
taken in by endocytosis. On the way to lysosomes, endocytosed
material must first pass through a series of endosomes.
Peroxisomes are small vesicular compartments that contain
enzymes used in various oxidative reactions.
The higher amount of organelles in larger (eukaryotic) cells can be
seen as an adaptation to increase in size the cell has a much
smaller SA:V ratio, and so its plasma membrane alone is too small
to sustain all the vital functions such as the pumping of ions, ATP
synthesis, protein secretion and lipid synthesis.

The above image is a suggested pathway for the evolution of the

eukaryotic cell and its internal membranes. It is thought that the
first eukaryotic cells arose when an ancient anaerobic archaeon
joined forces with an aerobic bacterium. As indicated, the nuclear
envelope may have originated form an invagination of the plasma
membrane of this archaeon. The chromosome was protected while
still allowing access of the DNA to the cytosol (to allow protein
synthesis). This envelope may have later pinched off completely
from the membrane, to create a separate compartment surrounded

by a double membrane. The nuclear compartment is topologically

equivalent to the cytosol because of the nuclear pores, and the
lumen of the ER (and all other organelles involved in the secretory
and endocytic pathways) is continuous with the space between the
inner and outer nuclear membranes, and is topologically equivalent
to the extracellular space.
The interiors of the organelles with the same topologically
equivalent compartments communicate extensively with one
another and the outside world via transport vesicles, which bud off

from one organelle and fuse with another.

The above image shows the topologically equivalent compartments
in the secretory and endocytic pathways in a eukaryotic cell. They
are considered topologically equivalent if they can communicate
with one another (molecules can get from one to the other without
having to cross a membrane). The spaces are shown in red, and the
communication mechanism is shown in A.
The evolutionary schemes group the intracellular compartments into
four distinct families:
1. The nucleus and the cytosol, which communicate with each
other through nuclear pore complexes and are topologically
continuous.
2. All organelles that function in the secretory and endocytic
pathways ER, Golgi apparatus, endosomes, lysosomes,
transport vesicles and peroxisomes.
3. The mitochondria
4. The plastids (chloroplasts and such in plants only).
The synthesis of all proteins begins on ribosomes in the cytosol,
except for the few that are synthetized on the ribosomes of
mitochondria and plastids. Their subsequent fate depends on their
amino acid sequences, which can contain sorting signals that

direct their delivery to locations outside the cytosol or to organelle

surfaces.
There are 3 fundamentally different ways by which proteins move
from one compartment to another.
1. Gated transport proteins and RNA
move between the cytosol and the
nucleus through nuclear pore
complexes in the nuclear envelope. The
pores function as selective gates that
support the active transport of specific
macromolecules, and allow free
diffusion of smaller molecules.
2. Protein translocation
transmembrane protein translocators
directly transport specific proteins
across a membrane from the cytosol
into a space that is topologically
distinct.
3. Vesicular transport membraneenclosed transport intermediates ferry
proteins from one topologically
equivalent compartment to another
(budding, shown below).

With budding, membrane is also transferred.

Also, the original orientation of both proteins
and lipids in the donor compartment
membrane is preserved in the target
compartment membrane. Thus, membrane
proteins retain their asymmetric orientation,
with the same domains always facing the
cytosol.

In multipass transmembrane proteins,

the polypeptide chain passes back and forth
repeatedly across the lipid bilayer as
hydrophobic a-helices. It is thought that an
internal signal sequence serves as a starttransfer signal in these proteins to initiate
translocation, which continues until the

translocator

encounters a stop-transfer sequence. In double-pass

transmembrane proteins, the polypeptide can then be released into
the bilayer.

In more complex multipass proteins, in which many hydrophobic ahelices span the bilayer, a second start-transfer sequences initiates
translocation further down the polypeptide chain until the next stoptransfer sequence causes polypeptide release, ad so forth.

In the above image, the insertion of the multipass membrane

protein rhodopsin into the ER membrane is shown. It is the lightsensitive protein in rod photoreceptor cells in the mammalian retina.
The hydrophobic region nearest the N-terminus serves as a starttransfer sequences, causing the preceding N-terminal portion of the
protein to pass across the ER membrane. Subsequent hydrophobic
sequences function in alteration as start-transfer and stop-transfer
sequences. The green arrows indicate the paired start and stop
signals inserted into the translocator. The final integrated rhodopsin
has its N-terminus located in the ER lumen and its C-terminus
located in the cytosol.