A biophysical model of how alpha-tubulin carboxy-terminal tails tune kinesin-1 processivity along microtubule
Само за регистроване кориснике
2017
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
It appears that so called post translational modifications of tubulin heterodimers are mostly focussed at positions of amino acid sequences of carboxy terminal tails. These changes have very profound effects on microtubule functions especially in connection with cellular traffic in terms of motor proteins. In this study, we elaborated the biophysical model aimed to explain the strategy governing these subtle interplays between structural and functional properties of microtubules. We relied onto Langevin equations including fluctuation dissipation processes. In that context we found out that small interaction between a charged motor neck domain and oppositely charged carboxy terminal tail of the a tubulin plays the decisive role in tuning kinesin-1 motor processivity along microtubules.
Кључне речи:
Cytoskeleton / Microtubule / Carboxy-terminal tails / Motor proteins / Kinesin-1 / Post-translational modificationsИзвор:
Journal of Theoretical Biology, 2017, 420, 152-157Финансирање / пројекти:
- Утицај елементарних ексцитација и конформација на физичка својства нових материјала базираних на јако корелисаним нискодимензионалним системима (RS-MESTD-Basic Research (BR or ON)-171009)
- Развој метода, сензора, и система за праћење квалитета воде, ваздуха и земљишта (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-43008)
- Provincial Secretariat for Higher Education and Scientific Research of AP Vojvodina [114-451-2708/2016-03]
DOI: 10.1016/j.jtbi.2017.03.012
ISSN: 0022-5193; 1095-8541
PubMed: 28300595
WoS: 000400952700016
Scopus: 2-s2.0-85015645339
Колекције
Институција/група
VinčaTY - JOUR AU - Satarić, Miljko V. AU - Sekulić, Dalibor L. AU - Zdravković, Slobodan AU - Ralević, Nebojša M. PY - 2017 UR - https://vinar.vin.bg.ac.rs/handle/123456789/1560 AB - It appears that so called post translational modifications of tubulin heterodimers are mostly focussed at positions of amino acid sequences of carboxy terminal tails. These changes have very profound effects on microtubule functions especially in connection with cellular traffic in terms of motor proteins. In this study, we elaborated the biophysical model aimed to explain the strategy governing these subtle interplays between structural and functional properties of microtubules. We relied onto Langevin equations including fluctuation dissipation processes. In that context we found out that small interaction between a charged motor neck domain and oppositely charged carboxy terminal tail of the a tubulin plays the decisive role in tuning kinesin-1 motor processivity along microtubules. T2 - Journal of Theoretical Biology T1 - A biophysical model of how alpha-tubulin carboxy-terminal tails tune kinesin-1 processivity along microtubule VL - 420 SP - 152 EP - 157 DO - 10.1016/j.jtbi.2017.03.012 ER -
@article{ author = "Satarić, Miljko V. and Sekulić, Dalibor L. and Zdravković, Slobodan and Ralević, Nebojša M.", year = "2017", abstract = "It appears that so called post translational modifications of tubulin heterodimers are mostly focussed at positions of amino acid sequences of carboxy terminal tails. These changes have very profound effects on microtubule functions especially in connection with cellular traffic in terms of motor proteins. In this study, we elaborated the biophysical model aimed to explain the strategy governing these subtle interplays between structural and functional properties of microtubules. We relied onto Langevin equations including fluctuation dissipation processes. In that context we found out that small interaction between a charged motor neck domain and oppositely charged carboxy terminal tail of the a tubulin plays the decisive role in tuning kinesin-1 motor processivity along microtubules.", journal = "Journal of Theoretical Biology", title = "A biophysical model of how alpha-tubulin carboxy-terminal tails tune kinesin-1 processivity along microtubule", volume = "420", pages = "152-157", doi = "10.1016/j.jtbi.2017.03.012" }
Satarić, M. V., Sekulić, D. L., Zdravković, S.,& Ralević, N. M.. (2017). A biophysical model of how alpha-tubulin carboxy-terminal tails tune kinesin-1 processivity along microtubule. in Journal of Theoretical Biology, 420, 152-157. https://doi.org/10.1016/j.jtbi.2017.03.012
Satarić MV, Sekulić DL, Zdravković S, Ralević NM. A biophysical model of how alpha-tubulin carboxy-terminal tails tune kinesin-1 processivity along microtubule. in Journal of Theoretical Biology. 2017;420:152-157. doi:10.1016/j.jtbi.2017.03.012 .
Satarić, Miljko V., Sekulić, Dalibor L., Zdravković, Slobodan, Ralević, Nebojša M., "A biophysical model of how alpha-tubulin carboxy-terminal tails tune kinesin-1 processivity along microtubule" in Journal of Theoretical Biology, 420 (2017):152-157, https://doi.org/10.1016/j.jtbi.2017.03.012 . .