Motor Proteins - Video Tutorials & Practice Problems
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Motor Proteins
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In this video, we're going to begin our discussion on motor proteins. So motor proteins actually create movement using the cytoskeleton. And so before we talk any more details about motor proteins, let's first do a quick recap on the cytoskeleton. So recall from way back in our previous lesson videos that the cytoskeleton consists of microfilaments, intermediate filaments, and microtubules. And so down below in the depiction of our cell here, you can see we've got the cell membrane. And inside of our cell, you can see a lot of different structures, including the different structures of the cytoskeleton. So you can see that we have microfilaments, we've got intermediate filaments, and we've got microtubules all within our cell. And really what these cytoskeleton components, function to do is, they function, to provide cell shape. So you can see that, here you can see the distribution of the cytoskeleton, in our cells. So they do provide cell shape. They also help to provide movement, of cells. And they can also provide transportation of molecules within the cell, and they can be involved in signaling as well because they can respond to external molecules and, that can cause, the cytoskeleton to shift inside. And so, this is going to be important to, remember the different components of, cytoskeletons because, different motor proteins will interact with different parts of the cytoskeleton. And so in our next lesson video, we'll be able to talk more about these motor proteins. So I'll see you guys in that video.
2
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Motor Proteins
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So now that we've briefly covered the cytoskeleton, we can focus more on motor proteins. And so motor proteins are going to be proteins themselves that use energy in the form of ATP, and they use the cytoskeleton as tracks in order to create molecular movement. Now, this molecular movement is responsible for muscle contractions which we'll talk a lot more about later in our course. They're also responsible for movements of individual cells through their environments and they're responsible for intracellular movement as well in terms of transportation of molecules and organelles within the cell. And we'll also be able to talk more about this idea as we move forward in our course. Now there are actually many different types of motor proteins, so we can't cover them all in this course, but some of the more well characterized motor proteins that your professors might expect you guys to know are myosin, kinesin, and dynein. And so we've got the structures of these three motor proteins down below. So the first one right here is myosin. The next one that we have here is Kinesen. And then last but not least, over here on the far right, we have dining And so as we move forward in our course, we'll be able to talk more about each of these 3 different motor proteins. But I can tell you now that these 3 motor proteins are gonna interact, with different components of the cytoskeleton. Myosin is gonna interact with microfilaments whereas kinesin and dynein are gonna interact with microtubules. And again, we'll be able to talk more about that as we move forward in our course starting with myosin. So I'll see you guys in our next video.
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Motor Proteins
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In this video, we're going to talk more about the motor protein myosin. So, myosin is specifically a motor protein that is going to move along thin actin microfilaments. And so myosin is responsible for transporting molecular cargo such as vesicles that might contain proteins or lipids or other macromolecules, and it's responsible for transporting this molecular cargo along the thin actin microfilaments. But the myosin protein, as we'll see later in our course, is also involved in muscle contractions. And so later when we talk more details about muscle contractions, we are going to see this myosin motor protein again. And so notice down below on the left hand side, we're showing you a single myosin molecule and notice that at the tips here, we have these pinkish structures that are referred to as the myosin heads. And then, this, rest of the chain right here is referred to as the myosin tails. And so what's important to note is that many myosin molecules can actually aggregate together to form thick filaments. And so, what you can see here, this arrow represents protein aggregation where we can take multiple myosin molecules and organize them in this fashion right here to create the thick myosin filament. And so, this entire structure that we see here is referred to as thick myosin filament. And again, we are going to see thick myosin filament again later in our course when we talk about muscle contraction. So be sure to remember, the structure of the myosin motor protein. And so this concludes our introduction to the myosin motor protein and in our next lesson video, we'll be able to talk about kinesin. So I'll see you guys in that Video.
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Motor Proteins
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In this video, we're going to talk about the motor protein kinesin, which interacts with microtubules. And so, it's important to know that microtubule subunits will actually assemble to make a polarized molecule with oppositely charged ends. And so if we take a look down below at our image, this microtubule right here that we see is a polarized molecule with oppositely charged ends. You can see that on the left hand side, it has the negatively charged end. And on the right hand side, it has a positively charged end. And so kinesin is going to be a motor protein that specifically moves towards the positively charged end of the microtubule. So it can transport and pull molecular cargos such as vesicles or chromosomes along the microtubules pulling the microtubule cargo, the molecular cargo towards the positively charged end of the microtubule. Now, as we'll see down below in our image, the kinesin heads are going to bind to the microtubule, motor protein. And notice that, the motor protein and notice that, the kinesin heads, which are down below here, are attached directly to the microtubule as we mentioned up above, and notice that the light chains, which are, pretty much right here, the kinesin light chains, are attached, to the molecular cargo, which is this vesicle up here. And so the kinesin motor protein is capable of pulling the vesicle or the molecular cargo towards the positively charged end of the microtubule. So, you can see that this arrow here represents the direction of movement towards the positively charged end. And also notice that the motor protein utilizes energy in the form of ATP in order to transport the molecular cargo. Now, if you haven't YouTubed kinesin, then it's definitely something that you wanna do because it's remarkable to see these depictions of the kinesin heads walking along the microtubule. So, for sure, if you've never googled kinesin or YouTube kinesin, make sure to YouTube kinesin so that you can get a better understanding of its movement along the microtubules. Now, one thing that helps me memorize the direction of Kinesen's movement which is towards the positively charged end of the microtubule. It is to note that, kin, which is found in the word kinesin, is a word that means family. And so up above, you can see that there's this nice looking family here that are all happy, and that is just something very positive. And so Kin, which is family, is very positive, and that reminds me that kinesin moves towards the positively charged end of the microtubule. And so, this concludes our lesson on Kinesin's movement towards the positively charged end of the microtubule And in our next lesson video, we'll be able to talk about, dynein and its interactions with the microtubule. So I'll see you guys in that video.
5
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Motor Proteins
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In this video, we're going to talk about the motor protein dynein which also interacts with the microtubule and really dynein is the opposite of the motor protein kinesin. And that's because dynein is a motor protein that specifically moves towards the negatively charged end of the microtubule. And so that's going to allow it to transport and pull molecular cargo, such as vesicles along the microtubules, but this time towards the negatively charged end of the microtubule, which is the opposite direction of kinesin. And so dynein is actually responsible for the motion of eukaryotic flagella and cilia. And so down below in our example here, you can see that we've got our microtubule, which is a polarized molecule with a negatively charged end and a positively charged end. And notice that our motor protein dynein here is actually moving in the opposite direction towards the negatively charged end over here. And so it also utilizes energy in the form of ATP to move, the vessel, the molecular cargo, again, towards the negatively charged end. And so one thing that helps me remember that dynein moves towards the negatively charged end of the microtubule is that dynein kinda sounds like dying. And so dying is death, and death is not a good thing, so it's a negative thing. And so noticing that dynein sounds like dying, reminds me that dynein moves towards the negatively charged end of the microtubule. And so this here concludes our lesson on how dynein moves towards the negatively charged end of the microtubule, and we'll be able to get some practice utilizing the concepts that we've learned as we move forward in our course. So I'll see you guys in our next video.
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Problem
Problem
What are the common features of the motor proteins kinesin and dynein?
A
Both types of motor proteins bind microtubules.
B
Both types of motor proteins bind and hydrolyze ATP.
C
Both types of motor proteins undergo conformational changes when they travel along the microtubule.
D
Both types of motor proteins 'step' from one tubulin subunit to another.
E
All of the above are true.
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Problem
Problem
Your lab isolates a new type of motor protein, which is some version of either myosin, kinesin, or dynein but it is unclear exactly what type it is. You hypothesize that the motor protein is NOT myosin. Which of the following is a piece of evidence that would support your hypothesis?
A
The protein was isolated by adding then purifying actin microfilaments that it was bound to.
B
The protein was isolated by adding then purifying microtubules that it was bound to.
C
The protein aggregated in solution.
D
The protein did not have a vesicle attached to it when purified.