n cell biology, the nucleus (pl.

 nuclei; from Latin nucleus or nuculeus, meaning kernel or seed) is

a membrane-bound organelle found in eukaryotic cells. Eukaryotes usually have a single nucleus,
but a few cell types, such as mammalian red blood cells, have no nuclei, and a few others
including osteoclasts have many.
The cell nucleus contains all of the cell's genome, except for a small fraction of mitochondrial DNA,
organized as multiple long linear DNA molecules in a complex with a large variety of proteins, such
as histones, to form chromosomes. The genes within these chromosomes are structured in such a
way to promote cell function. The nucleus maintains the integrity of genes and controls the activities
of the cell by regulating gene expression—the nucleus is, therefore, the control center of the cell.
The main structures making up the nucleus are the nuclear envelope, a double membrane that
encloses the entire organelle and isolates its contents from the cellular cytoplasm, and the nuclear
matrix (which includes the nuclear lamina), a network within the nucleus that adds mechanical
support, much like the cytoskeleton, which supports the cell as a whole.
Because the nuclear envelope is impermeable to large molecules, nuclear pores are required to
regulate nuclear transport of molecules across the envelope. The pores cross both nuclear
membranes, providing a channel through which larger molecules must be actively transported by
carrier proteins while allowing free movement of small molecules and ions. Movement of large
molecules such as proteins and RNA through the pores is required for both gene expression and the
maintenance of chromosomes. Although the interior of the nucleus does not contain any membrane-
bound subcompartments, its contents are not uniform, and a number of nuclear bodies exist, made
up of unique proteins, RNA molecules, and particular parts of the chromosomes. The best-known of
these is the nucleolus, which is mainly involved in the assembly of ribosomes. After being produced
in the nucleolus, ribosomes are exported to the cytoplasm where they translate mRNA.

Mitochondria [1] (sing. mitochondrion) are organelles, or parts of a eukaryote cell. They are in

the cytoplasm, not the nucleus.
They make most of the cell's supply of adenosine triphosphate (ATP), a molecule that cells use as a
source of energy. Their main job is to convert energy. They oxidise glucose to provide energy for the
cell. The process makes ATP, and is called cellular respiration.[2] This means mitochondria are
known as "the powerhouse of the cell"[3].
In addition to supplying cellular energy, mitochondria are involved in a range of other processes,
such as signalling, cellular differentiation, cell death, as well as the control of the cell division cycle
and cell growth.[4]
A lysosome (/ˈlaɪsəˌsoʊm/) is a membrane-bound organelle found in many animal cells.[1] They
are spherical vesicles that contain hydrolytic enzymes that can break down many kinds
of biomolecules. A lysosome has a specific composition, of both its membrane proteins, and
its lumenal proteins. The lumen's pH (~4.5–5.0)[2] is optimal for the enzymes involved in
hydrolysis, analogous to the activity of the stomach. Besides degradation of polymers, the
lysosome is involved in various cell processes, including secretion, plasma membrane repair, cell
signaling, and energy metabolism.[3]
Lysosomes digest materials taken into the cell and recycle intracellular materials. Step one shows material entering a food
vacuole through the plasma membrane, a process known as endocytosis. In step two a lysosome with an active hydrolytic
enzyme comes into the picture as the food vacuole moves away from the plasma membrane. Step three consists of the
lysosome fusing with the food vacuole and hydrolytic enzymes entering the food vacuole. In the final step, step four,
hydrolytic enzymes digest the food particles.[4]

Lysosomes act as the waste disposal system of the cell by digesting obsolete or un-used materials
in the cytoplasm, from both inside and outside the cell. Material from outside the cell is taken-up
through endocytosis, while material from the inside of the cell is digested through autophagy.
[5]
 The sizes of the organelles vary greatly—the larger ones can be more than 10 times the size of
the smaller ones.[6] They were discovered and named by Belgian biologist Christian de Duve,
who eventually received the Nobel Prize in Physiology or Medicine in 1974.
Lysosomes are known to contain more than 60 different enzymes, and have more than 50
membrane proteins.[7][8] Enzymes of the lysosomes are synthesised in the rough endoplasmic
reticulum. The enzymes are imported from the Golgi apparatus in small vesicles, which fuse with
larger acidic vesicles. Enzymes destined for a lysosome are specifically tagged with the
molecule mannose 6-phosphate, so that they are properly sorted into acidified vesicles.[9][10]
Synthesis of lysosomal enzymes is controlled by nuclear genes. Mutations in the genes for these
enzymes are responsible for more than 30 different human genetic disorders, which are
collectively known as lysosomal storage diseases. These diseases result from an accumulation of
specific substrates, due to the inability to break them down. These genetic defects are related to
several neurodegenerative disorders, cancers, cardiovascular diseases, and ageing-
related diseases.[11][12]
Lysosomes should not be confused with liposomes, or with micelles.

The Golgi apparatus, also known as the Golgi complex, Golgi body, or simply the Golgi, is

an organelle found in most eukaryotic cells.[1] It was identified in 1897 by the Italian scientist Camillo
Golgi and named after him in 1898.[2]
Part of the endomembrane system in the cytoplasm, the Golgi apparatus packages
proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their
destination. The Golgi apparatus resides at the intersection of the secretory, lysosomal,
and endocytic pathways. It is of particular importance in processing proteins for secretion, containing
a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move
through the apparatus.
The endoplasmic reticulum (ER) is a type of organelle found in eukaryotic cells that forms an
interconnected network of flattened, membrane-enclosed sacs or tube-like structures known
as cisternae. The membranes of the ER are continuous with the outer nuclear membrane. The
endoplasmic reticulum occurs in most types of eukaryotic cells, but is absent from red blood
cells and spermatozoa.
There are two types of ER: rough endoplasmic reticulum (RER) and smooth endoplasmic
reticulum (SER). The outer (cytosolic) face of the rough endoplasmic reticulum is studded
with ribosomes that are the sites of protein synthesis. The rough endoplasmic reticulum is especially
prominent in cells such as hepatocytes. The smooth endoplasmic reticulum lacks ribosomes and
functions in lipid synthesis but not metabolism, the production of steroid hormones,
and detoxification.[1] The smooth ER is especially abundant in mammalian liver and gonad cells.
The surface of the rough endoplasmic reticulum (often abbreviated RER or Rough ER) (also
called granular endoplasmic reticulum) is studded with protein-manufacturing ribosomes giving it a
"rough" appearance (hence its name).[8] The binding site of the ribosome on the rough endoplasmic
reticulum is the translocon.[9] However, the ribosomes are not a stable part of this organelle's
structure as they are constantly being bound and released from the membrane. A ribosome only
binds to the RER once a specific protein-nucleic acid complex forms in the cytosol. This special
complex forms when a free ribosome begins translating the mRNA of a protein destined for
the secretory pathway.[10] The first 5–30 amino acids polymerized encode a signal peptide, a
molecular message that is recognized and bound by a signal recognition particle (SRP). Translation
pauses and the ribosome complex binds to the RER translocon where translation continues with
the nascent (new) protein forming into the RER lumen and/or membrane. The protein is processed
in the ER lumen by an enzyme (a signal peptidase), which removes the signal peptide. Ribosomes
at this point may be released back into the cytosol; however, non-translating ribosomes are also
known to stay associated with translocons.[11]
The membrane of the rough endoplasmic reticulum forms large double membrane sheets that are
located near, and continuous with, the outer layer of the nuclear envelope.[12] The double membrane
sheets are stacked and connected through several right or left-handed helical ramps, the so-called
Terasaki ramps, giving rise to a structure resembling a multi-storey car park.[13][14] Although there is no
continuous membrane between the endoplasmic reticulum and the Golgi apparatus, membrane-
bound transport vesicles shuttle proteins between these two compartments.[15] Vesicles are
surrounded by coating proteins called COPI and COPII. COPII targets vesicles to the Golgi
apparatus and COPI marks them to be brought back to the rough endoplasmic reticulum. The rough
endoplasmic reticulum works in concert with the Golgi complex to target new proteins to their proper
destinations. A second method of transport out of the endoplasmic reticulum involves areas
called membrane contact sites, where the membranes of the endoplasmic reticulum and other
organelles are held closely together, allowing the transfer of lipids and other small molecules.[16][17]
The rough endoplasmic reticulum is key in multiple functions:

 Manufacture of lysosomal enzymes with a mannose-6-phosphate marker added in the cis-

Golgi network.[citation needed]
 Manufacture of secreted proteins, either secreted constitutively with no tag or secreted in a
regulatory manner involving clathrin and paired basic amino acids in the signal peptide.
 Integral membrane proteins that stay embedded in the membrane as vesicles exit and bind
to new membranes. Rab proteins are key in targeting the
membrane; SNAP and SNARE proteins are key in the fusion event.
 Initial glycosylation as assembly continues. This is N-linked (O-linking occurs in the Golgi).
o N-linked glycosylation: If the protein is properly
folded, Oligosaccharyltransferase recognizes the AA sequence NXS or NXT (with the S/T
 residue phosphorylated) and adds a 14-sugar backbone (2-N-acetylglucosamine, 9-
branching mannose, and 3-glucose at the end) to the side-chain nitrogen of Asn.
Smooth endoplasmic reticulum[edit]

Electromicrograph showing smooth ER (arrow) in mouse tissue, at 110,510 x magnification.

In most cells the smooth endoplasmic reticulum (abbreviated SER) is scarce. Instead there are
areas where the ER is partly smooth and partly rough, this area is called the transitional ER. The
transitional ER gets its name because it contains ER exit sites. These are areas where the transport
vesicles that contain lipids and proteins made in the ER, detach from the ER and start moving to
the Golgi apparatus. Specialized cells can have a lot of smooth endoplasmic reticulum and in these
cells the smooth ER has many functions.[6] It synthesizes lipids, phospholipids,[18][19][20] and steroids.
Cells which secrete these products, such as those in the testes, ovaries, and sebaceous
glands have an abundance of smooth endoplasmic reticulum.[21] It also carries out the metabolism of
carbohydrates, detoxification of natural metabolism products and of alcohol and drugs, attachment of
receptors on cell membrane proteins, and steroid metabolism.[22] In muscle cells, it regulates calcium
ion concentration. Smooth endoplasmic reticulum is found in a variety of cell types (both animal and
plant), and it serves different functions in each. The smooth endoplasmic reticulum also contains the
enzyme glucose-6-phosphatase, which converts glucose-6-phosphate to glucose, a step
in gluconeogenesis. It is connected to the nuclear envelope and consists of tubules that are located
near the cell periphery. These tubes sometimes branch forming a network that is reticular in
appearance.[12] In some cells, there are dilated areas like the sacs of rough endoplasmic reticulum.
The network of smooth endoplasmic reticulum allows for an increased surface area to be devoted to
the action or storage of key enzymes and the products of these enzymes.
Ribosomes (/ˈraɪbəˌsoʊm, -boʊ-/[1]) comprise a complex macromolecular machine, found within all
living cells, that serves as the site of biological protein synthesis (translation). Ribosomes link amino
acids together in the order specified by messenger RNA (mRNA) molecules. Ribosomes consist of
two major components: the small ribosomal subunits, which read the mRNA, and the large subunits,
which join amino acids to form a polypeptide chain. Each subunit consists of one or more ribosomal
RNA (rRNA) molecules and a variety of ribosomal proteins (r-protein or rProtein[2][3][4]). The ribosomes
and associated molecules are also known as the translational apparatus.

A vacuole (/ˈvækjuːoʊl/) is a membrane-bound organelle which is present in

all plant and fungal cells and some protist, animal[1] and bacterial cells.[2][verification needed] Vacuoles are
essentially enclosed compartments which are filled with water containing inorganic and organic
molecules including enzymes in solution, though in certain cases they may contain solids which
have been engulfed. Vacuoles are formed by the fusion of multiple membrane vesicles and are
effectively just larger forms of these.[3] The organelle has no basic shape or size; its structure varies
according to the requirements of the cell.