English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The role of phosphorylation and dephosphorylation of shell matrix proteins in shell formation : an in vivo and in vitro study

Du, J., Xu, G., Liu, C., & Zhang, R. (2018). The role of phosphorylation and dephosphorylation of shell matrix proteins in shell formation: an in vivo and in vitro study. CrystEngComm, 20(27), 3905-3916. doi:10.1039/C8CE00755A.

Item is

Files

show Files
hide Files
:
Article.pdf (Publisher version), 5MB
Name:
Article.pdf
Description:
-
OA-Status:
Hybrid
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Du, Jinzhe, Author
Xu, Guangrui, Author
Liu, Chuang1, Author           
Zhang, Rongqing, Author
Affiliations:
1Mason Dean (Indep. Res.), Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2231639              

Content

show
hide
Free keywords: -
 Abstract: Protein phosphorylation is a fundamental mechanism regulating many aspects of cellular processes. Shell matrix proteins (SMPs) control crystal nucleation, polymorphism, morphology, and organization of calcium carbonate crystallites during shell formation. SMPs phosphorylation is suggested to be important in shell formation but the mechanism is largely unknown. Here, to investigate the mechanism of phosphorylation of SMPs in biomineralization, we performed in vivo and in vitro experiment. By injection of antibody against the anti-phosphoserine/threonine /tyrosine into the extrapallial fluid of the pearl oyster Pinctada fucata, phosphorylation of matrix proteins were significantly reduced after 6 days. Newly formed prismatic layers and nacre tablet were found to grow abnormally with reduced crystallinity and possibly changed crystal orientation shown by Raman spectroscopy. In addition, regeneration of shells is also inhibited in vivo. Then, protein phosphatase was used to dephosphorylate SMPs extracted from the shells. After dephosphorylation, the ability of SMPs to inhibiting calcium carbonate formation have been reduced. Surprisingly, the ability of SMPs to modulate crystal morphology have been largely compromised although phosphorylation extent remained to be at least half of the control. Furthermore, dephosphorylation of SMPs changed the distribution of protein occlusions and decreased the amount of protein occlusions inside crystals shown by confocal imaging, indicating interaction between phosphorylated SMPs and crystals. Taken together, this study provides insight into the mechanism of phosphorylation of SMPs during shell formation.

Details

show
hide
Language(s):
 Dates: 2018-06-012018
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1039/C8CE00755A
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: CrystEngComm
  Other : CrystEngComm
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Royal Society of Chemistry
Pages: - Volume / Issue: 20 (27) Sequence Number: - Start / End Page: 3905 - 3916 Identifier: ISSN: 1466-8033