Phase transition of fibrillarin LC domain regulates localization and protein interaction of fibrillarin (Record no. 61950)

MARC details
000 -LEADER
fixed length control field 02442nam a2200205Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20251009160707.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-21860
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 251009s9999 xx 000 0 und d
245 10 - TITLE STATEMENT
Title Phase transition of fibrillarin LC domain regulates localization and protein interaction of fibrillarin
490 0# - SERIES STATEMENT
Series statement Biochemical Journal, 478(4), 799-810, 2021
500 ## - GENERAL NOTE
General note Artículo
520 3# - SUMMARY, ETC.
Summary, etc. A key nucleolar protein, fibrillarin, has emerged as an important pharmacological target as its aberrant expression and localization are related to tumorigenesis, chemoresistance and poor survival in breast cancer patients. Fibrillarin contains a N-terminal low complexity sequence (LC) domain with a skewed amino acid distribution, which is known to undergo a phase transition to liquid-like droplets. However, the underlying mechanism of the phase transition of the fibrillarin LC domain and its physiological function are still elusive. In this study, we show that the localization of fibrillarin and its association with RNA binding proteins is regulated by this phase transition. Phenylalanine-to-serine substitutions of the phenylalanine:glycine repeats in the fibrillarin LC domain impede its phase transition into liquid-like droplets, as well as the hydrogel-like state composed of polymers, and also its incorporation into hydrogel or liquid-like droplets composed of wild-type LC domains. When expressed in cultured cells, fibrillarin containing the mutant LC domain fails to localize to the dense fibrillar component of nucleoli in the same way as intact fibrillarin. Moreover, the phase transition of the fibrillarin LC domain is required for the interaction of fibrillarin with other RNA binding proteins, such as FUS, TAF15, DDX5 and DHX9. Taken together, the results suggest that the phenylalanine residues in the LC domain are critical for the phase transition of fibrillarin, which in turn regulates the sub-nucleolar localization of fibrillarin and its interaction with RNA binding proteins, providing a useful framework for regulating the function of fibrillarin.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element FIBRILLARIN;LC DOMAIN;PHASE TRANSITION;NUCLEOLUS;RNA BINDING PROTEINS
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Kim, E.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Kwon, I.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1LbLHps8664maCoSsTl_pEmWJSDEmX_0U/view?usp=drive_link">https://drive.google.com/file/d/1LbLHps8664maCoSsTl_pEmWJSDEmX_0U/view?usp=drive_link</a>
Public note Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
Holdings
Lost status Source of classification or shelving scheme Damaged status Not for loan Collection Home library Current library Shelving location Date acquired Total checkouts Full call number Date last seen Price effective from Koha item type
  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 09.10.2025   B-21860 09.10.2025 09.10.2025 Documentos solicitados