Cell and Molecular Biology

Membrane Proteins
A membrane protein is any protein found in a biological membrane. They
participate in various biological processes, such as cell signaling-transduction pathways.
The membrane proteins also play a strong role in controlling a wide array of gradients such
as chemical, electrical, and mechanical gradients and are responsible for cell structure
during key cell events such as division. Due to their many functions in the membrane, they
are in high concentration on the surface of the membrane. They may also act as channels
that move specific molecules into and out of the membrane. These proteins fall into two
main categories, depending upon how strongly the protein interacts with the membrane.1
The two main categories are listed below:
 Integral proteins are permanently attached to the membrane and are typically
transmembrane (they span across the bilayer)
 Peripheral proteins are temporarily attached by non-covalent interactions and
associate with one surface of the membrane

Membrane proteins can serve a variety of key functions:

 Junctions – Serve to connect and join two cells together
 Enzymes – Fixing to membranes localises metabolic pathways
 Transport – Responsible for facilitated diffusion and active transport
 Recognition – May function as markers for cellular identification
 Anchorage – Attachment points for cytoskeleton and extracellular matrix
 Transduction – Function as receptors for peptide hormones 2

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Spectrin
Spectrin is a large, cytoskeletal, and heterodimeric protein composed of modular
structure of α and β subunits, it typically contains 106 contiguous amino acid sequence
motifs called “spectrin repeats”. Spectrin is crucial for maintaining the stability and
structure of the cell membrane and the shape of a cell. Moreover, it contributes to diverse
cell functions such as cell adhesion, cell spreading, and the cell cycle.
Spectrin is a cytoskeletal protein that was first discovered in erythrocytes and is
important for maintaining the stability, structure, and shape of the cell membrane. Spectrin
forms a complex two-dimensional intracellular network by interacting with intracellular
proteins such as actin, ankyrin, and adducin. This network maintains the flexibility and
shape of the cell membrane.

Spectrin is multifunctional, and spectrin-based networks are important for

maintaining the shape and mechanical properties of cells. Deletion of spectrin coding
sequences seriously impairs cell adhesion and spreading. Spectrin also interacts with the
Gogli apparatus to manage intracellular traffic.3

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Ankyrin
Ankyrins are a family of scaffolding proteins that link the membrane-bound proteins
to the underlying cytoskeleton. This function of ankyrins contributes to the expression,
specific localization, and overall stability of membrane proteins within the plasma
membrane.4
Ankyrins, together with their spectrin partners are responsible for micron-scale
organization of vertebrate plasma membranes, including those of erythrocytes, excitable
membranes of neurons and heart, lateral membrane domains of columnar epithelial cells,
and striated muscle. Ankyrins coordinate functionally related membrane transporters and
cell adhesion proteins (15 protein families identified so far) within plasma membrane
compartments through independently evolved interactions of intrinsically disordered
sequences.5
In most eukaryotic cells, it serve as adaptor proteins that link membrane proteins to
the underlying cytoskeleton. These adaptor proteins form protein complexes consisting of
integral membrane proteins, signalling molecules and cytoskeletal components. With their
modular architecture and ability to interact with many proteins, ankyrins organize and
stabilize these protein networks, thereby establishing the infrastructure of membrane
domains with specialized functions. To this end, ankyrin collaborates with a number of
proteins including cytoskeletal proteins, cell adhesion molecules and large structural
proteins.6

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Actin
Actin is a highly conserved, key cytoskeletal protein involved in numerous
structural and functional roles. Although actin is present throughout the cell, it is most
highly concentrated in the region close to the plasma membrane. As a broad generalization,
actin can be thought of as forming a peripheral layer around the cell, like an elastic stocking
or a muscular skin. This layer, known as the cell cortex, gives the outer surface of the cell
the mechanical strength and enables it to move.8
The major cytoskeletal protein of most cells is actin, which polymerizes to form
actin filaments—thin, flexible fibers approximately 7 nm in diameter and up to several
micrometers in length. Within the cell, actin filaments (also called microfilaments) are
organized into higher-order structures, forming bundles or three-dimensional networks
with the properties of semisolid gels. The assembly and disassembly of actin filaments,
their crosslinking into bundles and networks, and their association with other cell
structures (such as the plasma membrane) are regulated by a variety of actin-binding
proteins, which are critical components of the actin cytoskeleton. Actin filaments are
particularly abundant beneath the plasma membrane, where they form a network that
provides mechanical support, determines cell shape, and allows movement of the cell
surface, thereby enabling cells to migrate, engulf particles, and divide.9

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Cell and Molecular Biology

Bacteriorhodopsin
Bacteriorhodopsin is a membrane protein with light-driven proton pump activity
found in the purple membrane of Halobacterium salinarum. Bacteriorhodopsin is the
simplest proton pump that, on in vivo absorption of light, cause a pH decrease of the
outside cell medium.10 It converts the energy of "green" light (500-650 nm, max 568 nm)
into an electrochemical proton gradient, which in turn is used for ATP production by ATP
synthase. It functions as a light-driven proton pump, transporting protons out of the cell,
and exemplifies vectorial catalysis.
Bacteriorhodopsin - as all retinal proteins
from Halobacterium - folds into a seven-
transmebrane helix topology with short
interconnecting loops. The helices (named A-G) are
arranged in an arc-like structure and tightly
surround a retinal molecule that is covalently
bound via a Schiff base to a conserved lysine (Lys-
216) on helix G.11
The surface of Halobacterium salinarum
contains membrane patches called the purple
membrane. The protein:lipid ratio is 75:25. The
only protein in the purple membrane is
bacteriorhodopsin which forms a hexagonal 2-
dimensional crystal consisting of bacteriorhodopsin
trimers.
The purple membrane can be easily isolated
and permits mass production of bacteriorhodopsin
as is required for biotechnological applications. 11

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Porins
Porins are beta barrel proteins that cross a cellular membrane and act as a pore,
through which molecules can diffuse. Unlike other membrane transport proteins, porins
are large enough to allow passive diffusion, i.e., they act as channels that are specific to
different types of molecules. They are present in the outer membrane of gram-negative
bacteria and some gram-positive Mycobacteria
A typical porin is a trimer of β barrels trans membrane proteins that act as a
specific pore or channel large enough to allow passive diffusion. These are partially block
by a loop, called the eyelet, which profects in to the cavity to determine the size of molecule
to traverse the channel.
These are found in mitochondria, chloroplast and in the external membrane of bacteria.
Porins are especially useful in the regulation of diffusion regarding small molecular
weighted metabolits such as sugars, amino acids and ions.12

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Selectins
Selectins are a group of cell adhesion molecules that are glycoproteins and play an
important role in the relationship of circulating cells to the endothelium. The members of
this surface molecule family have three separate structural motifs. They have a single N-
terminal (extracellular) lectin motif preceding a single epidermal growth factor repeat and
various short consensus repeat homology units. They are involved in lymphocyte
migration. These carbohydrate-binding proteins facilitate adhesion of leukocytes to
endothelial cells. There is a single chain transmembrane glycoprotein in each of the selectin
molecules with a similar modular structure that includes an extracellular calcium-
dependent lectin domain. There are three separate groups of selectins:

 L-selectin (CD62L), expressed on leukocytes

 P-selectin (CD62P), expressed on platelets and
activated endothelium
 E-selectin (CD62E), expressed on activated
endothelium

Under shear forces their characteristic structural

motif is comprised of an N-terminal lectin domain, a
domain with homology to epidermal growth factor
(EGF) and various complement regulatory protein
repeat sequences.13

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References
1. n.a. c2000. Structural Biochemistry/Membrane Proteins. From
https://en.wikibooks.org/w/index.php?title=Structural_Biochemistry/Membrane_P
roteins&stable=1
2. n.a. n.d. Membrane Proteins. From http://ib.bioninja.com.au/standard-level/topic-
1-cell-biology/13-membrane-structure/membrane-proteins.html
3. Zang et al. 2012. Spectrin: Structure, function and disease. from
https://link.springer.com/article/10.1007/s11427-013-4575-0
4. Vaidyanathan et al. 2014. Scaffolding Proteins and Iom Channel Diseases. From
https://www.sciencedirect.com/science/article/pii/B9781455728565000236
5. Kline, C.F. Mohler, P. 2013. Functional Organization of Vertebrate Plasma
Membrane. From https://www.sciencedirect.com/topics/biochemistry-genetics-
and-molecular-biology/ankyrin
6. Cunha, S. Mohler. 2009. Ankyrin protein networks in membrane formation and
stabilization. From https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4515052/
7. Low, P.S. 2009. Where spectrin snuggles with ankyrin. From
http://www.bloodjournal.org/content/113/22/5372/tab-figures-only?sso-
checked=true
8. n.a. n.d. Actin and Membranes. From
https://www.google.com/url?sa=t&rct=j&q=&esrc=s&source=web&cd=11&cad=rja
&uact=8&ved=2ahUKEwj9hsTO4LngAhUDiXAKHY1yCr0QFjAKegQIBxAB&url=https
%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fbooks%2FNBK9908%2F&usg=AOvVaw1L
TlZWODb3_cAadN9-RFar
9. Cooper & Sunderland. 2000. The Cell: A Molecular Approach. 2nd edition. From
https://www.ncbi.nlm.nih.gov/books/NBK9908/
10. Barnadas, et al. 2003. Liposomes Prepared by High-Pressure Homogenizers. From
https://www.sciencedirect.com/science/article/pii/S0076687903670047
11. Oesterhelt, D. nd. BR – Bacteriorhodopsin. From
https://www.biochem.mpg.de/523002/Protein_BR
12. Lets Talk Academy. Porins in Cell Membrane. From
https://www.letstalkacademy.com/publication/read/porins-in-cell-membrane
13. n.a. 2004. Immunology Guidebook. 1 – Molecules, Cells, and Tissues of Immunity.
From
https://www.sciencedirect.com/science/article/pii/B978012198382650025X

* All websites were accessed on February 14, 2019.

*n.a. – No named author
*n.d. – No specified date of publication