NDLI: Novel Mechanism of Regulation of Protein 4.1G Binding Properties Through Ca$^{2+}$/Calmodulin-Mediated Structural Changes

Content Provider	Springer Nature Link
Author	Numura, Wataru Jinbo, Yuji Isozumi, riyoshi Ohki, Shinya Izumi, Yoshibu Matsushima, rio Takakuwa, Yuichi
Copyright Year	2013
Abstract	Protein 4.1G (4.1G) is a widely expressed member of the protein 4.1 family of membrane skeletal proteins. We have previously reported that Ca$^{2+}$-saturated calmodulin (Ca$^{2+}$/CaM) modulates 4.1G interactions with transmembrane and membrane-associated proteins through binding to Four.one-ezrin–radixin–moesin (4.1G FERM) domain and N-terminal headpiece region (GHP). Here we identify a novel mechanism of Ca$^{2+}$/CaM-mediated regulation of 4.1G interactions using a combination of small-angle X-ray scattering, nuclear magnetic resonance spectroscopy, and circular dichroism spectroscopy analyses. We document that GHP intrinsically disordered coiled structure switches to a stable compact structure upon binding of Ca$^{2+}$/CaM. This dramatic conformational change of GHP inhibits in turn 4.1G FERM domain interactions due to steric hindrance. Based upon sequence homologies with the Ca$^{2+}$/CaM-binding motif in protein 4.1R headpiece region, we establish that the 4.1G S$^{71}$RGISRFIPPWLKKQKS peptide (pepG) mediates Ca$^{2+}$/CaM binding. As observed for GHP, the random coiled structure of pepG changes to a relaxed globular shape upon complex formation with Ca$^{2+}$/CaM. The resilient coiled structure of pepG, maintained even in the presence of trifluoroethanol, singles it out from any previously published CaM-binding peptide. Taken together, these results show that Ca$^{2+}$/CaM binding to GHP, and more specifically to pepG, has profound effects on other functional domains of 4.1G.
Starting Page	545
Ending Page	558
Page Count	14
File Format	PDF
ISSN	10859195
Journal	Cell Biochemistry and Biophysics
Volume Number	66
Issue Number	3
e-ISSN	15590283
Language	English
Publisher	Springer US
Publisher Date	2013-01-26
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Calmodulin Protein 4.1G Intrinsic disorder SAXS NMR CD Biochemistry Pharmacology/Toxicology Biotechnology Cell Biology Biophysics and Biological Physics
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Biochemistry Biophysics

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1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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