| 
  • If you are citizen of an European Union member nation, you may not use this service unless you are at least 16 years old.

  • You already know Dokkio is an AI-powered assistant to organize & manage your digital files & messages. Very soon, Dokkio will support Outlook as well as One Drive. Check it out today!

View
 

Aylah-Clark

Page history last edited by amclark1@edisto.cofc.edu 15 years ago

 

 

Myosin

 

                                                                                                                        

 

 

 

 

Introduction

 

     Myosin is a motor protein that has many functional roles but plays an integral part in muscle functioning and cytokinesis. Myosin works closely with actin, using ATP to move along actin filaments in muscle fibers. There are approximately 20 classes of myosin which are apparent in its rather dendritic phylogenetic tree. These different types of myosin are coded for by at least 39 genes currently identified in the human genome. Myosin is categorized by differences in its structure.

 

Video on General Muscle Contraction

 


 

Structure

 

     The basic structure of myosin includes head, neck, and tail domains. The globular head, also known as the motor domain, consists of Actin and ATP-binding sites and is found in every heavy chain. The heavy chain can also include a neck. The neck is the joint in which the head is bound to the tail and can serve as a binding site for a light chain. The tail interacts with other molecules and can help mediate myosin activity. The structure and function of these domains can be very diverse. Although they have many commonalities, some differences include direction of movement, velocity, regulation techniques, and variations in its primary movement called the powerstroke.

 

Shown below are the structures of several of the most common forms of myosin:

 

  

Myosin I                             Myosin II

 

                  

      Myosin III                     Myosin V                      Myosin VI

 

     

    Myosin VII                     Myosin IX

 


 

Mechanism

 

     Although different forms of myosin have subtle differences in the execution of its movement or powerstroke, a more general description can encompass the approach used by most myosins.

 

The Power Stroke:

     -As the head attaches to an actin filament by ATP hydrolysis, ADP is released causing a conformational change in they myosin to a cocked position mounted on the actin.

 

          File:Myosin powerstroke.JPG

    

      -When a new ATP binds the head of the myosin it is released from the actin filament

     -The actin filament does not return to its original position at this point due to the attachment of many other myosin proteins

 

YouTube plugin error

 

Video on Myosin Mechanism


 

Current/Future Research

 

    There is extensive current research on myosin such as exploring the role of myosin in linking actin cytoskeleton with cell membranes and studying the mechanism of a reverse recovery-step in myosin II mechanism. Research on the myosin protein has revealed links between myosin deficiencies and diseases such as hypertrophy of the heart, sarcomeric defects such as heart enlargement, and problems with blood platelets. Usher 1B syndrome is caused by a defect in myosin VIIA and results in deafness and blindness.  With future research it may be possible to cure the diseases and understand more about muscle function and causes of muscle dystrophy.

 

 

 

 

Comments (1)

Christopher Korey said

at 10:32 pm on Apr 6, 2009

Looks good. As you convert the outline to text, Remember to be concise about each subsection and provide link outs to other pages or papers that provide more in depth detail if that is required. If someone wants more information give them a way to find it not necessarily put it on the page--for example I embed one of the movies and link out to the others. Try to divide the sections by inserting a horizontal bar. Remember to reference just like any other paper, images as well.

You don't have permission to comment on this page.