Page 233 - Color Atlas of Biochemistry
P. 233
224 Organelles
Membrane receptors B. Insulin receptor
The receptor for the hormone insulin (see
To receive and pass on chemical or physical
signals, cells are equipped with receptor pro- p. 76) belongs to the family of 1-helix recep-
tors.
teins. Many of these are integral membrane
These molecules span the membrane with
proteins in the plasma membrane, where only one α-helix. The subunits of the dimeric
they receive signals from their surroundings.
Other receptor proteins are located in inter- receptor (red and blue) each consist of two
polypeptides (α and β)bound by disulfide
cellular membranes. The receptors for lipo-
philic hormones are among the few that func- bonds. The α-chains together bind the insulin,
tion in a soluble form. They regulate gene while the β-chains contain the transmem-
brane helix and, at the C-terminus, domains
transcription in the nucleus (see p. 378).
with tyrosine kinase activity. In the activated
state, the kinase domains phosphorylate
A. Principle of receptor action themselves and also mediator proteins (re-
ceptor substrates) that set in motion cascades
Membrane-located receptors can be divided of further phosphorylations (see pp. 120 and
into three parts, which have different tasks.
The receptor domain reacts specifically to a 388).
given signal. Signals of this type can be of a
purely physical nature. For example, many C. 7-helix receptors
organisms react to light. In this way, plants A large group of receptors span the mem-
adapt growth and photosynthesis to light
conditions, while animals need light recep- brane with α-helices seven times. These are
tors for visual processing (C; see p. 358). Me- known as 7-helix receptors. Via their effector
domains, they bind and activate trimeric pro-
chanoreceptors are involved in hearing and in
pressure regulation, among other things. teins, which in turn bind and hydrolyze GTP
and are therefore called G proteins. Most G
Channels that react to action potentials (see
p. 350) can be regarded as receptors for elec- proteins, in turn, activate or inhibit enzymes
trical impulses. that create secondary signaling molecules
However, most receptors do not react to (second messengers; see p. 386). Other G pro-
physical stimuli, but rather to signal mole- teins regulate ion channels. The illustration
cules. Receptors for these chemical signals shows the complex of the light receptor rho-
containbinding sites inthe receptor domain dopsin, with the associated G protein trans-
that are complementary to each ligand. In this ducin (see p. 358). The GTP-binding α-subunit
(green) and the γ-subunit (violet) of transdu-
respect, they resemble enzymes (see p. 94).
As the effector domain of the receptor is usu- cin are anchored in the membrane via lipids
(see p. 214). The β-subunit is shown in detail
ally separated by a membrane, a mechanism
for signal transfer between the domains is on p. 72.
needed. Little is yet known regarding this. It
is thought that conformation changes in the D. T-cell receptor
receptor protein play a decisive part. Some
receptors dimerize after binding of the ligand, The cells of theimmunesystem communicate
thereby bringing the effector domains of two with each other particularly intensively. The
molecules into contact (see p. 392). T-cell receptor plays a central role in the acti-
vation of T lymphocytes (see p. 296). The cell
The way in which the effector works differs
from case to case. By binding or interconver- at the top has been infected with a virus, and
it indicates this by presenting a viral peptide
sion, many receptors activate special media-
tor proteins, which then trigger a signal cas- (violet) with the help of a class I MHC protein
cade (signal transduction; see p. 384). Other (yellow and green). The combination of the
two molecules is recognized by the dimeric
receptors function as ion channels.This is
particularly widespread in receptors for neu- T-cell receptor (blue) and converted into a
rotransmitters (see p. 354). signal that activates the T cell (bottom) and
thereby enhances the immune response to
the virus.
Koolman, Color Atlas of Biochemistry, 2nd edition © 2005 Thieme
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