ATP11C DEFICIENCY AND

ANEMIA IN MICE
By:
Muhammad Rifki Ramadhan
Nindia Safaat
Putri Azhari
Vina Detri Kirana

FOUR MAJOR PHOSPHOLIPIDS IN

MAMMALIAN PLASMA MEMBRANES
Concentrated in outer
layer
Phosphatidylcholine
Sphingomyelin
Concentrated in inner
layer
Phosphatidylethanolami
ne
Phosphatidylserine

PHOSPHATYDIL SERINE
Phosphatidylserine
Phospholipid membrane component
Plays a key role in cell cycle
signaling
Actively held facing thecytosolic
side of the cell membrane by the
enzymeflippase
Are negatively charged

ATP11C
ATP11C
ATP11Cis anenzymethat is
encoded by theATP11Cgene
ATP11C is a major flippase in
human and other mammals
erythrocytes
Catalyzes transfer of
phosphatidylserin to cytosolic
monolayer
Maintain asimetric plasma
membrane structure

ATP11C DEFICIENCY
Stomatocyt
es

Anemi
a
Vesicle
Trafficking
Defect

Reduced
Cells
Lifespan

RED BLOOD CELLS

Figure of Human red blood cells have a characteristic flattened biconcave shape, as seen in this
scanning electron
Micrograph (second picture). (Essenstial Cell Biology fourth edition)

RED BLOOD CELLS

The cortex of human red blood
cells is a relatively simple and
regular structure and has been
especially well studied. These
cells are small and have a
distinctive flattened shape The
main component of their
cortex is the dimeric protein
spectrin, a long, thin, flexible
rod about 100 nm in length. It
forms a meshwork that
provides support for the
plasma membrane and
maintains the cells biconcave

A SPECTRIN MESHWORK FORMS THE CELL

CORTEX IN HUMAN RED BLOOD CELLS.
A spectrin meshwork forms the cell cortex in
human red blood cells. Spectrin dimers are linked
end-to-end to
form longer tetramers. The spectrin tetramers,
together with a smaller number of actin molecules,
are linked together into a mesh. This network is
attached to the plasma membrane by the binding
of at least two types of attachment proteins
(shown here in yellow and blue) to two kinds of
transmembrane proteins (shown here in green and
brown). Electron micrograph showing the spectrin
meshwork on the cytoplasmic side of a red blood
cell membrane. The meshwork has been stretched
out to show the details of its structure; in the
normal cell, the meshwork shown would be much
more crowded and would occupy only about onetenth of this area. (B, courtesy of T. Byers and D.
Branton, Proc. Natl. Acad. Sci. USA 82:61536157,
1985. With permission from the National Academy
of Sciences.)