MOLECULAR

MOTOR Proteins
Presented by- Haimanti Nath
ID No.- 58540
Course- Nanotechnology
Course code- BMB 641
Table of Contents-
 Definition
 Types of motor proteins
 Structure of different motor proteins
 Function of motor proteins
 Mechanism of action of different motor proteins
INTRODUCTION:-
Definition:
 Motor proteins are a class of molecular
motors that can move along the cytoplasm
of cells.
 These remarkable proteins bind to a polarized
cytoskeletal filament and use the energy derived
from repeated cycles of ATP hydrolysis to move
steadily along it. Fig: Kinesin motor moving on
microtubule using protein
dynamics on nanoscale
Types of motor proteins:-
 In animal and fungal cells, motor proteins utilizing the cytoskeleton for movement
fall into two categories based on their substrate ; either microfilaments or
microtubules.
i. Actin motors: These motors move along microfilaments through interaction
with actin microfilament. E.g.- Myosin motor protein.
ii. Microtubule motors: These motors move along microtubules through
interaction with tubulin. E.g.- Kinesin and Dynein motor proteins.
Continued………..
 Microtubule motors, again can be of two types- plus-end motors and minus-end
motors, depending on the direction in which they move along the microtubule
cables within the cell.

Fig: Plus-end
motor and
Minus-end
motor
Fig: Microtubule structure
Continued…..
Plant specific motors:-
 The cells of flowering plants lack dynein motors. However, they contain a larger
number of different kinesins.
 Many of these plant-specific kinesin groups are specialized for functions during
plant cell mitosis.
 During mitosis, the new cell wall is built by the formation of a cell plate starting in
the center of the cell. This process is facilitated by a phragmoplast, a microtubule
array unique to plant cell mitosis. The building of cell plate and ultimately the new
cell wall requires kinesin-like motor proteins.
Structure of different Motor
proteins:-
Myosin motor protein:-
 The first motor protein identified was skeletal
muscle protein Myosin, which is responsible
for generating the force for muscle contraction
in animal skeletal muscle cells.
 This Myosin named Myosin II, one of the
members of Myosin superfamily, is an
elongated protein that is formed from two
heavy chains and two copies of each of two
light chains.
 Each of the heavy chains has a globular head
domain at its N-terminus that contains the
force-generating machinery, followed by a
very long amino acid sequence that forms an
extended coiled-coil that mediates heavy chain Fig: (A) A myosin II molecule
dimerization. The two light chains bind close (B) Electron micrographs of myosin molecules
to the N-terminal head domain. shadowed with platinum
Continued…
 The long coiled-coil tail bundles
itself with the tails of other myosin
molecules.
 These tail-tail interactions result in
the formation of large bipolar “thick
filaments” that have several hundred
myosin heads, oriented in opposite
directions at the two ends of the
thick filament.

Fig: (A) Electron micrograph of a myosin II thick filament isolated from frog
muscle.
(B) The myosin II molecules aggregate by means of their tail regions, with their
heads projecting to the outside of the filament.
(C) A small section of a myosin II filament as reconstructed from electron
micrographs.
Kinesin motor protein:-
 Kinesin is a motor protein that moves along microtubules.
 Kinesin is similar structurally to myosin II in having two heavy chains and two light
chains per active motor, two globular head motor domains, and an elongated coiled-coil
responsible for heavy chain dimerization.
 Like myosin, kinesin is a member of a large protein superfamily, for which the motor
domain is the only common element.
 Conventional kinesin has the motor domain at the N-terminus of the heavy chain. The
middle domain forms a long coiled-coil, mediating dimerization. The C-terminal domain
forms a tail that attaches to cargo, such as a membrane-enclosed organelle.
Continued…..
 KIFC2 is a member of a family of C-terminal
kinesins. These kinesins generally travel in the
opposite direction from the majority of kinesins,
toward the minus end instead of the plus end of a
microtubule.
 KIF2 has its motor domain located in the middle of
the heavy chain. It is a member of a family of
kinesins that have lost typical motor activity and
instead bind to microtubule ends to increase dynamic
instability of microtubules.
 KIF1B is a member of the unusual class of kinesins
that seem to function as monomers and move
membrane-enclosed organelles along microtubules.
Fig: (B) Freeze-etch electron micrograph
of a kinesin molecule with the head
domains on the left.
Dynein motor protein:-
 The dyneins are a family of minus-end-directed
microtubule motors.
 They are composed of two or three heavy chains
(that include the motor domain) and a large and
variable number of associated light chains.
Dyneins are the largest of the known molecular
motors, and they are also among the fastest.
 The dynein family has two major branches:
Cytoplasmic Dynein and Axonemal Dynein.
 Cytoplasmic dyneins are important for vesicle
trafficking, as well as for localization of the Golgi Fig: Axonemal/Ciliary Dynein
apparatus near the center of the cell. Axonemal
dyneins are highly specialized for the rapid and
efficient sliding movements of microtubules that
drive the beating of cilia and flagella.
Cytoplasmic Dynein:-
 Dynein belongs to the AAA+ superfamily (ATPases associated with diverse activities).
 Like conventional AAA+ ATPases, dynein has a ring of six AAA+ modules at its core
but, unusually, these are linked together into one large polypeptide, along with several
unique appendages that enable motor function.
 Each heavy chain contains a motor domain that belongs to the AAA+ superfamily
attached to a divergent amino-terminal tail domain. The tail specifies distinct
oligomerization properties and serves as a platform for the binding of several types of
associated subunit, which in turn mediate interactions with cargo either via direct
binding or through the recruitment of adaptor proteins.
Fig: a) Linear representation of domains within the dynein heavy chain. b) Cytoplasmic
Dynein complex association. c) A 3D model of the cytoplasmic dynein motor domain bound
to the microtubule (the associated subunits are not shown)
Function of motor proteins:-
 Motor proteins are the driving force behind most active transport of proteins and
vesicles in the cytoplasm.
 Kinesin and cytoplasmic dyneins play essential roles in intracellular transport such
as axonal transport and in the formation of the spindle apparatus and the
separation of the chromosomes during mitosis and meiosis.
 Axonemal dynein, found in cilia and flagella, is crucial to cell motility, for
example in spermatozoa, and fluid transport, for example in trachea.
 The muscle protein myosin regulates the contraction of muscle fibers in animals.
 Mechanism of action of
different motor proteins:-
 Myosin motor protein:

Fig: The cycle of

structural changes
used by myosin to
walk along an actin
filament
Kinesin motor protein:

Fig: Mechanochemical cycle of Kinesin action

 Dynein motor protein:

Fig: Model of the

mechanochemical cycle
of a cytoplasmic dynein
motor domain
Nano motor:-
 By mimicking energy conversion procedure of the biological motor
proteins, different nano motors have been synthesized artificially.
 A nanomotor is a molecular or nanoscale device capable of
converting energy into movement. It can typically generate forces
on the order of piconewtons.
Application:-
 Nano motors are used in biosensing.
 Nano motors are used in cardiovascular disease therapy.
 Nano motors are used in tumor therapy in humans.
 Nano motors are also used in site specific drug delivery inside
human body.
References:
 Hirokawa N, Takemura R (October 2003). "Biochemical and molecular characterization of
diseases linked to motor proteins". Trends in Biochemical Sciences. 28 (10): 558–65.
doi:10.1016/j.tibs.2003.08.006. PMID 14559185.
 Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002-01-01). "Molecular Motors".
NCBI - National Institutes of Health.
 Roberts AJ, Kon T, Knight PJ, Sutoh K, Burgess SA (November 2013). "Functions and mechanics
of dynein motor proteins". Nature Reviews. Molecular Cell Biology. 14 (11): 713–26.
doi:10.1038/nrm3667. PMC 3972880. PMID 24064538.
 Hartman MA, Spudich JA (April 2012). "The myosin superfamily at a glance". Journal of Cell
Science. 125 (Pt 7): 1627–32. doi:10.1242/jcs.094300. PMC 3346823. PMID 22566666
 Verhey KJ, Kaul N, Soppina V (2011-01-01). "Kinesin assembly and movement in cells". Annual
Review of Biophysics. 40: 267–88. doi:10.1146/annurev-biophys-042910-155310. PMID
21332353