지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2021.8
- 수록면
- 591 - 601 (11page)
- DOI
- 10.14348/molcells.2021.0082
이용수
초록· 키워드
오류제보하기
Cilia are highly specialized organelles that extend from the cell membrane and function as cellular signaling hubs. Thus, cilia formation and the trafficking of signaling molecules into cilia are essential cellular processes. TULP3 and Tubby (TUB) are members of the tubby-like protein (TULP) family that regulate the ciliary trafficking of G-protein coupled receptors, but the functions of the remaining TULPs (i.e., TULP1 and TULP2) remain unclear. Herein, we explore whether these four structurally similar TULPs share a molecular function in ciliary protein trafficking. We found that TULP3 and TUB, but not TULP1 or TULP2, can rescue the defective cilia formation observed in TULP3-knockout (KO) hTERT RPE-1 cells. TULP3 and TUB also fully rescue the defective ciliary localization of ARL13B, INPP5E, and GPR161 in TULP3 KO RPE-1 cells, while TULP1 and TULP2 only mediate partial rescues. Furthermore, loss of TULP3 results in abnormal IFT140 localization, which can be fully rescued by TUB and partially rescued by TULP1 and TULP2. TUB’s capacity for binding IFT-A is essential for its role in cilia formation and ciliary protein trafficking in RPE-1 cells, whereas its capacity for PIP2 binding is required for proper cilia length and IFT140 localization. Finally, chimeric TULP1 containing the IFT-A binding domain of TULP3 fully rescues ciliary protein trafficking, but not cilia formation. Together, these two TULP domains play distinct roles in ciliary protein trafficking but are insufficient for cilia formation in RPE-1 cells.
In addition, TULP1 and TULP2 play other unknown molecular roles that should be addressed in the future.
목차
등록된 정보가 없습니다.
참고문헌 (43)
참고문헌 신청
Ansley, S. J. / 2003 / Basal body dysfunction is a likely cause of pleiotropic Bardet–Biedl syndrome / Nature 425:628~633
Badgandi, H. B. / 2017 / Tubby family proteins are adapters for ciliary trafficking of integral membrane proteins / J. Cell Biol 216:743~760
Christensen, S. T. / 2007 / Sensory cilia and integration of signal transduction in human health and disease / Traffic 8:97~109
Colbert, H. A. / 1997 / OSM-9, a novel protein with structural similarity to channels, is required for olfaction, mechanosensation, and olfactory adaptation in Caenorhabditis elegans / J. Neurosci 17:8259~8269
Cole, D. G. / 1998 / Chlamydomonas kinesin-II–dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons / J. Cell Biol. 141:993~1008
Badgandi, H. B. / 2017 / Tubby family proteins are adapters for ciliary trafficking of integral membrane proteins / J. Cell Biol 216:743~760
Christensen, S. T. / 2007 / Sensory cilia and integration of signal transduction in human health and disease / Traffic 8:97~109
Colbert, H. A. / 1997 / OSM-9, a novel protein with structural similarity to channels, is required for olfaction, mechanosensation, and olfactory adaptation in Caenorhabditis elegans / J. Neurosci 17:8259~8269
Cole, D. G. / 1998 / Chlamydomonas kinesin-II–dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons / J. Cell Biol. 141:993~1008
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