Related Experiment Video
Updated: Feb 22, 2026
09:17
Author Spotlight: Unraveling the Role of Myosin-7a and Usher Proteins in Hearing and Human Disease
Published on: August 23, 2024
990
MYO18A: An unusual myosin
Matthew D Buschman1, Seth J Field1
1Department of Medicine, Division of Endocrinology and Metabolism, University of California, San Diego, La Jolla, CA 92093, USA.
Advances in Biological Regulation
|September 25, 2017
Summary
Myosin 18A (MYO18A) is a unique protein involved in intracellular transport and actin dynamics. This myosin is essential in higher organisms and implicated in cancer, though its motor activity remains unclear.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Myosin 18A (MYO18A) is a distinct myosin family member featuring an N-terminal PDZ domain.
- MYO18A participates in various intracellular transport mechanisms.
- Its precise motor functions are not fully elucidated.
Purpose of the Study:
- To summarize the known functions and characteristics of Myosin 18A (MYO18A).
- To highlight MYO18A's role in intracellular transport and its association with other proteins.
- To discuss MYO18A's potential implications in cancer biology.
Main Methods:
- Literature review of studies investigating MYO18A.
- Analysis of protein complex interactions involving MYO18A.
- Examination of MYO18A's role in cellular processes like actin dynamics and membrane trafficking.
Main Results:
- MYO18A forms complexes with LURAP1/MRCK for actin retrograde treadmilling.
- It collaborates with PAK2/βPIX/GIT1 for transport from focal adhesions to the leading edge.
- MYO18A interacts with GOLPH3 to facilitate Golgi-to-plasma membrane vesicle budding.
Conclusions:
- MYO18A is a versatile myosin essential for higher organisms.
- Its involvement in the GOLPH3 pathway suggests a role in cancer.
- Further research is needed to determine MYO18A's intrinsic motor activity.
Related Concept Videos
01:15Overview of Myosin Structure and Function
6.9K
Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X) have been well...
6.9K
01:08The Sarcomere
17.1K
A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each...
Each...
17.1K
01:16Actin and Myosin in Muscle Contraction
25.4K
Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
25.4K
01:10The Role of Actin and Myosin in Non-muscle Cells
5.2K
Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They are held...
5.2K
01:18Role of Myosin in Cell Migration
3.4K
Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
Myosin II is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction....
Myosin II is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction....
3.4K
01:26Introduction to Actin
6.7K
Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution. Actin coding genes are conserved within species and across...
6.7K