Trends in Biochemical Sciences
Volume 24, Issue 4, 1 April 1999, Pages 130-132
Protein SequenceSTART: a lipid-binding domain in StAR, HD-ZIP and signalling proteins
Section snippets
Acknowledgments
CPP is a National Research Council (USA) Senior Associate.
References (19)
Curr. Biol.
(1995)J. Biol. Chem.
(1998)BioEssays
(1996)- et al.
Proc. Natl. Acad. Sci. U. S. A.
(1998) Nucleic Acids Res.
(1997)- et al.
EMBO J.
(1995) Eur. J. Biochem.
(1980)- et al.
Eur. J. Biochem.
(1979) - et al.
Eur. J. Biochem.
(1986)
There are more references available in the full text version of this article.
Cited by (356)
HD-Zip IV transcription factors: Drivers of epidermal cell fate integrate metabolic signals
2023, Current Opinion in Plant BiologyNon-vesicular glycerolipids transport in plant cells
2022, Advances in Botanical ResearchTumor suppressor gene DLC1: Its modifications, interactive molecules, and potential prospects for clinical cancer application
2021, International Journal of Biological MacromoleculesCitation Excerpt :Furthermore, the first three amino acids were found to be critical for the binding to DLC1 [113]. The START domain containing 200–210 amino acids participates in lipid metabolism and transfer by binding a large number of lipids and sterols [74,114,115]. The START domain is located at the C-terminus of DLC1 and is critical for DLC1-mediated inhibition of actin stress fiber formation and growth [14].
Published by Elsevier Ltd.