Ubiquitination of Proteins

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[@chrisb833]

I'm glad you are making videos again! They are always super informative!

[@molecularunity]

Such a great vid, thank you. As always from AK Lectures, absolute clarity!

[@leavesandbud11]

This guy is getting me thru my senior year. Thanks AK lectures!!!

[@tanvirlatif3203]

Incredibly simple explanation, thank you so much!

[@LuisaElea]

Thank you so much for this video! It saved me fromt the sheer desperation caused by the un-explained diagrams concerning this topic on the slides our professor for biochemistry gave us. Oh, and second compliment to you(r work): It was perfectly easy to follow your explanations even as a non-native speaker. I guess, your account will be my lifeline this semester!

[@RohitPant04]

Quite helpful especially because of the notes you've prepared. ThankYou!

[@Bl4ckiii]

Thank you so much!! Finally, after hearing it in at least three different courses over the last few years, I got it 😁🍀👍

[@dilarakarabulak5673]

Thank you for this amazing explanation , it helped me a lot to grasp the consept really well .

[@victoriaegedus8075]

Such a great, thorough explanation, thank you!!!!

[@dhiaawad6710]

very very helpful. really appreciate it. I have Biochem and my prof. lecture sooo confusing. thank you.

[@saunyboy123]

The god of Biochemistry is back! I Love your videos so much!

[@ckwrp7rniui]

Thank you so much! You don't know how many times you've saved my life. Bless your soul.

[@hamedhosseini4938]

The god of knowledge is back! we love you! keep up the content!!

[@shripadchitnis2782]

Good job dude ! You are a very good teacher ! Keep going ...

[@brunochannel1]

Valeu, irmão. Explicação bem objetiva e clara. Thanks!!! =)

[@suinberlin7227]

amazing video as always!!!

[@user-kx5jm3pk3t]

Thank you so much
You are really talented!

[@jamil6429]

thank you so much for this!

[@kelsiwillis6102]

Thank you so much for this video!

[@asgharalisabri2845]

Very good lecture to explain the Ubiquitination. but I have a question that how can it cause the many diseases or how can we use it as bookmarks for the therapeutic agent for different diseases????????

[@rosechemutaikoech8441]

I didn't know the use of ubiquitin thanks for that

[@baharmanhoush3742]

A Perfect explanation👌🏼

[@n3873]

You're literally the best

[@richardmiles9190]

Good message

[@amitmahindra40]

Thanks, very good explanation

[@imeneaida3515]

how does the ubiquitin identify and recognize the targeted protein ?

[@johnbates2709]

Is any research happening to understand how or why the ubiquitin system goes wrong and if there are potentially non-pharmacological or more natural approaches might be used to improve its function?

[@berilkocak859]

Good haircut.Sıhhatler olsun sağolasın.

[@palwindersingh1398]

Same my professor explained 😅 thx for revision 😇

[@balqis7559]

Thank you so much

[@sophiale1208]

Thank you !!

[@ashutoshpandey1797]

Thank U Guru JI

[@backstreetfan2887]

amazing

[@safwanbarnawi9743]

man you are awesome !!! thank you sooooooooooo much !!

[@gogomoh5909]

thank you

[@miheretusamuel9276]

very clear lecture thanks

[@khalidbhat9932]

thanks

[@ramchandrasuthar2848]

very nice & analytical lecture
Thanks

[@Sure.Not.]

Holy moly this video just made me realize even more just how much I don’t know…

[@usmanahmed3173]

than you so much!!

[@alexandra95789]

thx!

[@junczhang]

thanks!

[@bslaozora]

Thanks for the clear explanation. I have a question that I thought would naturally (?) arise:
What if the protein, say a very small one, doesn't have lysine in its composition? Or it's not possible because lysine is so common?
Thank you!

[@backstreetfan2887]

I just took a look at the wikipedia article for ubiquitin and it says it is actually possible for ubiquitin to get added to the N-terminus. It says it may also be possible for it to get added to cysteine, threonine, and serine. But addition to lysine is what is common or typical.

[@malak2858]

But what's the location of proteasome in the cell ?

[@user-hw9bh9ro3t]

amazing lecture as always ,so first step is reversible and the other 2,3 are irreversible

[@yvonnes7874]

How do Ubiquitin and CoQ10 relate, please?

[@aasthadubey6653]

Sir plz make a video on N-end rule pathway plzzzzz!!!!

[@SHUBHAMSINGH-ur5bm]

these topics are of which class in foreign because in India some topics are not there in 11 and 12 class

[@Villymanillyvoop]

Thank you. Quick question: How does the process 'know' when a protein needs breaking down? Is there a signalling pathway that gets activated to target the protein that needs breaking down?

[@bhapree4407]

Same question here. How does this marker gets the signal from the target protein

[@ChristinaKurtzer]

​@@bhapree4407 The short answer: We are not entirely sure.
The long answer: We are not entirely sure, but one piece of the puzzle that research has uncovered is something called "degrons" which are portions of a protein that alter the rate at which said protein is degraded either through the ubiquitin-proteasome pathway or a different protein-degradation pathway. As such, degrons are classified as either "ubiquitin-independent" or "ubiquitin-dependent" depending on whether or not the degron regulates protein degradation via the ubiquitin-proteasome pathway.
The rate of protein degradation increases when degrons are added to a protein and decreases when degrons are removed from a protein. Degrons can be certain amino acid sequences, motifs, certain secondary structures and many other things. Some degrons lead to faster protein degradation than others.
The exact mechanism by which ubiquitin-dependent degrons regulate protein degradation via the ubiquitin-proteasome pathway and why different degrons lead to different rates of ubiquitylation is poorly understood and an area of active research. Degrons are just one piece of the complex puzzle, and it is suspected that there are many other factors involved in the regulation of ubiquitylation besides the presence of ubiquitin-dependent degrons in a protein that have not yet been discovered.

[@cxpectations]

Nice!!!

[@Lightagon]

You're the best man!

[@AKLECTURES]

thanks!

[@lushka4706]

thank you soo much!!

[@zahraawaleed4596]

thank you soooooooooooooooooooooooo much🌸🌸🌸

[@devanshusingla7312]

thanks!!!

[@melinazamani7020]

You were talking about glycine then you moved onto lysine.. where did lysine come from? #confused

[@julian7518]

The lysine is located in the target protein, whereas glycine is part of the carboxyl terminal group of the ubiqitin. They are the two partners that form the isopeptide bond.

[@MohammedAli-ih5jx]

Melina Zamani lyللل

[@abinashbeherabiology9578]

I have a doubt how many types of proteasom are there in human cells

[@hotdecaffeinatedcoffee]

Masterrrrr Thankssssss

[@estherbovril510]

omg...it finally sink in my brain

[@biru5051]

Do this mechanism acts when we need to break down muscle protein to do gluconeogenesis, or just when proteins has defects?

[@adwambo9041]

Leonardo This occurs mostly when we have proteins which didn’t fold well or when we need to switch off a signalling pathway. Autophagy is the one linked to metabolism AFAIK.

[@biru5051]

Polo Wambo so autophagy breaks muscle protein into aminoacids so the gluconeogenesis can occur?

[@adwambo9041]

@@biru5051 both produce peptides at the end, which can be used for metabolism, but I think autophagy is switched on when there is low energy in the cell

[@sallycha7952]

Thank you so much! Best explanation!

[@rockstar-ep4oh]

Confused

[@sagargwal1192]

Sir i have doubt on some points

[@mariocavazos376]

my man what's up with your sleeve?

[@shaistello9786]

why are there any dislikes on this?

[@ShreyUniverse]

Proteolysis and Ubiquitination are different ?! :/ 😌

[@hassansofiat3117]

In 2021😘

[@02Inam]

awesome

[@AKLECTURES]

thanks!

[@austinhollingsworth2910]

Voice is sooo boring

[@mablemuk]

Not it is interesting