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91Ó°ÊÓ

There are no known motor proteins that move on intermediate filaments. Suggest an explanation for this.

Short Answer

Expert verified
Intermediate filaments lack polarity and dynamic assembly, making them unsuitable for motor protein movement.

Step by step solution

01

Understanding Motor Proteins

Motor proteins are molecular machines that convert chemical energy into mechanical work by hydrolyzing ATP. They typically move along cytoskeletal structures, such as microtubules and actin filaments, not intermediate filaments.
02

Analyzing the Structure of Intermediate Filaments

Intermediate filaments provide structural support and mechanical resistance to cells. They are more stable and less dynamic than microtubules and actin filaments, which are constantly being assembled and disassembled.
03

Consider the Suitability for Motor Protein Movement

Motor proteins require a track with uniform polarity and dynamic assembly, like microtubules or actin filaments, to move effectively. Intermediate filaments lack such polarity and undergo minimal dynamic assembly.
04

Explanation Summary

Without polarity, intermediate filaments do not provide a directional path for motor proteins. The stability and lack of dynamic assembly in intermediate filaments also do not meet the functional requirements necessary for motor protein movement.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Cytoskeletal Structures
The cytoskeleton is a complex network of fibers that spans the cytoplasm of eukaryotic cells. It serves multiple functions, including
  • maintaining cell shape
  • offering support and stability
  • enabling intracellular transport and cell division.
The main components of the cytoskeleton are microtubules, actin filaments, and intermediate filaments. Each type of filament plays distinct roles and has unique properties. While microtubules and actin filaments are dynamic and provide tracks for motor proteins, intermediate filaments offer structural reinforcement and resist mechanical stress. This diversity in structure and function ensures that a cell can perform and regulate an array of activities essential for its survival and proper functioning.
Intermediate Filaments
Intermediate filaments are one of the key structural elements of the cytoskeleton, yet they differ significantly from the other cytoskeletal structures, such as microtubules and actin filaments.

They are composed of a variety of proteins, depending on the cell type, allowing them to fulfil versatile roles in different tissues. They provide mechanical support and resist tensile forces, essentially helping cells maintain their integrity under stress.

Intermediate filaments are not as dynamic as microtubules and actin filaments, meaning they are more stable and less frequently assembled and disassembled. These filaments lack polarity, which is why they do not support the movement of motor proteins, as these proteins require a uniform directional track to function effectively. Instead, the primary role of intermediate filaments is in maintaining structural stability within the cell.
ATP Hydrolysis
ATP hydrolysis is a critical chemical process where ATP, or adenosine triphosphate, is broken down into ADP, or adenosine diphosphate, and an inorganic phosphate (Pi")). This reaction releases energy that can be harnessed by cells to perform various types of work, including muscle contraction, molecule synthesis, and cellular transport.

Motor proteins, such as kinesin and dynein, rely on the energy released from ATP hydrolysis to move along cytoskeletal tracks like microtubules. This process changes the conformation of the motor protein, prompting it to "walk" along the filament.
  • The hydrolysis of ATP is thus fundamental to the functionality of motor proteins.
  • It provides the necessary energy for cellular movement and transport processes to occur efficiently.
Without ATP hydrolysis and the proper cytoskeletal structures to move on, motor proteins could not perform their essential roles within the cell.
Structural Support in Cells
Cells are subject to various mechanical forces, and to withstand these forces, they require structural support. This support is provided by the cytoskeleton, with intermediate filaments playing a crucial role. They act like a scaffolding system within the cell, helping to maintain its shape and prevent deformation in response to mechanical pressure.

The robust nature of intermediate filaments allows them to withstand compressive and tensile stresses, providing resilience.
  • This structural reinforcement is essential for the overall functionality and survival of the cell.
  • While they do not serve as tracks for motor proteins due to their lack of polarity and dynamic assembly, they are indispensable for maintaining cellular integrity under physical stress.
The presence of these filaments throughout a cell underscores the importance of robust structural support in allowing cells to adapt to their environment and perform their wide range of functions effectively.

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Most popular questions from this chapter

The drug Taxol, extracted from the bark of yew trees, has an opposite effect to the drug colchicine, an alkaloid from autumn crocus. Taxol binds tightly to microtubules and stabilizes them; when added to cells, it causes much of the free tubulin to assemble into microtubules. In contrast, colchicine prevents microtubule formation. Taxol is just as pernicious to dividing cells as colchicine, and both are used as anticancer drugs. Based on your knowledge of microtubule dynamics, suggest why both drugs are toxic to dividing cells despite their opposite actions.

Why do you suppose it is much easier to add tubulin to existing microtubules than to start a new microtubule from scratch? Explain how \(\gamma\) -tubulin in the centrosome helps to overcome this hurdle.

Complete the following sentence accurately, explaining your reason for accepting or rejecting each of the four phrases (more than one can be correct). The role of calcium in muscle contraction is: A. To detach myosin heads from actin. B. To spread the action potential from the plasma membrane to the contractile machinery. C. To bind to troponin, cause it to move tropomyosin, and thereby expose actin filaments to myosin heads. D. To maintain the structure of the myosin filament.

The locomotion of fibroblasts in culture is immediately halted by the drug cytochalasin, whereas colchicine causes fibroblasts to cease to move directionally and to begin extending lamellipodia in seemingly random directions. Injection of fibroblasts with antibodies to vimentin has no discernible effect on their migration. What do these observations suggest to you about the involvement of the three different cytoskeletal filaments in fibroblast locomotion?

Which of the following statements are correct? Explain your answers. A. Kinesin moves endoplasmic reticulum membranes along microtubules so that the network of ER tubules becomes stretched throughout the cell. B. Without actin, cells can form a functional mitotic spindle and pull their chromosomes apart but cannot divide. C. Lamellipodia and filopodia are "feelers" that a cell extends to find anchor points on the substratum that it will then crawl over. D. GTP is hydrolyzed by tubulin to cause the bending of flagella. E. Cells having an intermediate-filament network that cannot be depolymerized would die. F. The plus ends of microtubules grow faster because they have a larger GTP cap. G. The transverse tubules in muscle cells are an extension of the plasma membrane, with which they are continuous; similarly, the sarcoplasmic reticulum is an extension of the endoplasmic reticulum. H. Activation of myosin movement on actin filaments is triggered by the phosphorylation of troponin in some situations and by \(\mathrm{Ca}^{2+}\) binding to troponin in others.

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