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Dual Facets of Drosophila melanogaster Cryptochrome: Unveiling Interactions With Jetlag for Timeless Degradation and Hyperkinetic in Neuronal Signaling
Dual Facets of Drosophila melanogaster Cryptochrome: Unveiling Interactions With Jetlag for Timeless Degradation and Hyperkinetic in Neuronal Signaling
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20250211152036
- ISBN
- 9798384049135
- DDC
- 574
- 서명/저자
- Dual Facets of Drosophila melanogaster Cryptochrome: Unveiling Interactions With Jetlag for Timeless Degradation and Hyperkinetic in Neuronal Signaling
- 발행사항
- [Sl] : Cornell University, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 137 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 86-03, Section: B.
- 주기사항
- Advisor: Crane, Brian.
- 학위논문주기
- Thesis (Ph.D.)--Cornell University, 2024.
- 초록/해제
- 요약Entrainment, the synchronization of internal circadian clocks with external light-dark cycles, is crucial for optimal organismal function. In Drosophila melanogaster, the flavoprotein cryptochrome (CRY) plays a central role in light-induced entrainment. CRY initiates the degradation of Timeless (TIM), a key clock protein, for clock resetting. Despite extensive research on CRY's role in TIM degradation, the intricate molecular mechanisms remain unclear. This dissertation focuses on the mechanistic details of Jetlag (JET), an E3 ubiquitin ligase, in mediating TIM degradation by CRY.We established a robust expression system for all components of the CRY:TIM:JET complex. Utilizing Select Western-blot Free Tagged-protein Interaction (SWFTI) assays to map protein-protein interactions, we comprehensively characterized their interactions, paving the way for subsequent purification and structural analysis. Notably, we identified a conserved JET binding site on CRY, similar to that observed in mammalian CRY:JET interactions. Intriguingly, our investigation uncovered a non-canonical role for CRY. SWFTI assays revealed an interaction between CRY and the voltage-gated potassium ion channel β-subunit, Hyperkinetic (HK). Unlike other known CRY interactions in the canonical clock, this novel CRY:HK interaction appears to be independent of light or cofactor binding. This dual functionality of CRY, mediating both circadian light entrainment and potentially influencing neuronal activity through HK, suggests a broader role for CRY in brain function.
- 일반주제명
- Biochemistry
- 일반주제명
- Molecular biology
- 일반주제명
- Neurosciences
- 기타저자
- Cornell University Biochemistry Molecular and Cell Biology
- 기본자료저록
- Dissertations Abstracts International. 86-03B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■00520250211152036
■006m o d
■007cr#unu||||||||
■020 ▼a9798384049135
■035 ▼a(MiAaPQ)AAI31335408
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a574
■1001 ▼aDeOliveira, Cristina Caseiro.▼0(orcid)0000-0002-1666-5934
■24510▼aDual Facets of Drosophila melanogaster Cryptochrome: Unveiling Interactions With Jetlag for Timeless Degradation and Hyperkinetic in Neuronal Signaling
■260 ▼a[Sl]▼bCornell University▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a137 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 86-03, Section: B.
■500 ▼aAdvisor: Crane, Brian.
■5021 ▼aThesis (Ph.D.)--Cornell University, 2024.
■520 ▼aEntrainment, the synchronization of internal circadian clocks with external light-dark cycles, is crucial for optimal organismal function. In Drosophila melanogaster, the flavoprotein cryptochrome (CRY) plays a central role in light-induced entrainment. CRY initiates the degradation of Timeless (TIM), a key clock protein, for clock resetting. Despite extensive research on CRY's role in TIM degradation, the intricate molecular mechanisms remain unclear. This dissertation focuses on the mechanistic details of Jetlag (JET), an E3 ubiquitin ligase, in mediating TIM degradation by CRY.We established a robust expression system for all components of the CRY:TIM:JET complex. Utilizing Select Western-blot Free Tagged-protein Interaction (SWFTI) assays to map protein-protein interactions, we comprehensively characterized their interactions, paving the way for subsequent purification and structural analysis. Notably, we identified a conserved JET binding site on CRY, similar to that observed in mammalian CRY:JET interactions. Intriguingly, our investigation uncovered a non-canonical role for CRY. SWFTI assays revealed an interaction between CRY and the voltage-gated potassium ion channel β-subunit, Hyperkinetic (HK). Unlike other known CRY interactions in the canonical clock, this novel CRY:HK interaction appears to be independent of light or cofactor binding. This dual functionality of CRY, mediating both circadian light entrainment and potentially influencing neuronal activity through HK, suggests a broader role for CRY in brain function.
■590 ▼aSchool code: 0058.
■650 4▼aBiochemistry
■650 4▼aMolecular biology
■650 4▼aNeurosciences
■653 ▼aOptimal organismal function
■653 ▼aKey clock protein
■653 ▼aProtein-protein interactions
■690 ▼a0487
■690 ▼a0307
■690 ▼a0317
■71020▼aCornell University▼bBiochemistry, Molecular and Cell Biology.
■7730 ▼tDissertations Abstracts International▼g86-03B.
■790 ▼a0058
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17162635▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
