PMID- 34831238
OWN - NLM
STAT- MEDLINE
DCOM- 20211227
LR  - 20231213
IS  - 2073-4409 (Electronic)
IS  - 2073-4409 (Linking)
VI  - 10
IP  - 11
DP  - 2021 Nov 4
TI  - Fine-Tuning of mTOR mRNA and Nucleolin Complexes by SMN.
LID - 10.3390/cells10113015 [doi]
LID - 3015
AB  - Increasing evidence points to the Survival Motor Neuron (SMN) protein as a key 
      determinant of translation pathway. Besides its role in RNA processing and 
      sorting, several works support a critical implication of SMN in ribosome 
      biogenesis. We previously showed that SMN binds ribosomal proteins (RPs) as well 
      as their encoding transcripts, ensuring an appropriate level of locally 
      synthesized RPs. SMN impacts the translation machinery in both neural and 
      non-neural cells, in agreement with the concept that SMN is an essential protein 
      in all cell types. Here, we further assessed the relationship between SMN and 
      translation-related factors in immortalized human fibroblasts. We focused on 
      SMN-nucleolin interaction, keeping in mind that nucleolin is an RNA-binding 
      protein, highly abundant within the nucleolus, that exhibits a central role in 
      ribosomes production. Nucleolin may also affects translation network by binding 
      the mammalian target of rapamycin (mTOR) mRNA and promoting its local synthesis. 
      In this regard, for the first time we provided evidence that SMN protein itself 
      associates with mTOR transcript. Collectively, we found that: (1) SMN coexists 
      with nucleolin-mTOR mRNA complexes at subcellular level; (2) SMN deficiency 
      impairs nucleolar compartmentalization of nucleolin, and (3) this event 
      correlates with the nuclear retention of mTOR mRNA. These findings suggest that 
      SMN may regulate not only structural components of translation machinery, but 
      also their upstream regulating factors.
FAU - Gabanella, Francesca
AU  - Gabanella F
AD  - CNR-Institute of Biochemistry and Cell Biology, Department of Sense Organs, 
      Sapienza University of Rome, Viale del Policlinico, 155-00161 Rome, Italy.
AD  - CNR-Institute of Molecular Biology and Pathology, Department of Molecular 
      Medicine, Sapienza University of Rome, Viale Regina Elena, 291-00161 Rome, Italy.
FAU - Barbato, Christian
AU  - Barbato C
AUID- ORCID: 0000-0003-1737-9064
AD  - CNR-Institute of Biochemistry and Cell Biology, Department of Sense Organs, 
      Sapienza University of Rome, Viale del Policlinico, 155-00161 Rome, Italy.
FAU - Fiore, Marco
AU  - Fiore M
AD  - CNR-Institute of Biochemistry and Cell Biology, Department of Sense Organs, 
      Sapienza University of Rome, Viale del Policlinico, 155-00161 Rome, Italy.
FAU - Petrella, Carla
AU  - Petrella C
AUID- ORCID: 0000-0003-0651-1816
AD  - CNR-Institute of Biochemistry and Cell Biology, Department of Sense Organs, 
      Sapienza University of Rome, Viale del Policlinico, 155-00161 Rome, Italy.
FAU - de Vincentiis, Marco
AU  - de Vincentiis M
AD  - Department of Sense Organs, Sapienza University of Rome, Viale del Policlinico, 
      155-00161 Rome, Italy.
FAU - Greco, Antonio
AU  - Greco A
AD  - Department of Sense Organs, Sapienza University of Rome, Viale del Policlinico, 
      155-00161 Rome, Italy.
FAU - Minni, Antonio
AU  - Minni A
AD  - Department of Sense Organs, Sapienza University of Rome, Viale del Policlinico, 
      155-00161 Rome, Italy.
FAU - Corbi, Nicoletta
AU  - Corbi N
AD  - CNR-Institute of Molecular Biology and Pathology, Department of Molecular 
      Medicine, Sapienza University of Rome, Viale Regina Elena, 291-00161 Rome, Italy.
FAU - Passananti, Claudio
AU  - Passananti C
AD  - CNR-Institute of Molecular Biology and Pathology, Department of Molecular 
      Medicine, Sapienza University of Rome, Viale Regina Elena, 291-00161 Rome, Italy.
FAU - Di Certo, Maria Grazia
AU  - Di Certo MG
AD  - CNR-Institute of Biochemistry and Cell Biology, Department of Sense Organs, 
      Sapienza University of Rome, Viale del Policlinico, 155-00161 Rome, Italy.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20211104
PL  - Switzerland
TA  - Cells
JT  - Cells
JID - 101600052
RN  - 0 (Phosphoproteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (SMN Complex Proteins)
RN  - EC 2.7.11.1 (TOR Serine-Threonine Kinases)
SB  - IM
MH  - Cell Line
MH  - Cell Nucleolus/metabolism
MH  - Gene Knockdown Techniques
MH  - Humans
MH  - Phosphoproteins/*metabolism
MH  - Protein Binding
MH  - Protein Biosynthesis
MH  - RNA, Messenger/genetics/metabolism
MH  - RNA-Binding Proteins/*metabolism
MH  - SMN Complex Proteins/deficiency/*metabolism
MH  - Subcellular Fractions/metabolism
MH  - TOR Serine-Threonine Kinases/*genetics/metabolism
MH  - Nucleolin
PMC - PMC8616268
OTO - NOTNLM
OT  - RNA translation
OT  - SMN
OT  - mTOR
OT  - nucleolin
OT  - nucleolus
OT  - padlock
OT  - ribosome biogenesis
COIS- The authors declare no conflict of interest.
EDAT- 2021/11/28 06:00
MHDA- 2021/12/28 06:00
PMCR- 2021/11/04
CRDT- 2021/11/27 01:14
PHST- 2021/09/09 00:00 [received]
PHST- 2021/10/28 00:00 [revised]
PHST- 2021/11/02 00:00 [accepted]
PHST- 2021/11/27 01:14 [entrez]
PHST- 2021/11/28 06:00 [pubmed]
PHST- 2021/12/28 06:00 [medline]
PHST- 2021/11/04 00:00 [pmc-release]
AID - cells10113015 [pii]
AID - cells-10-03015 [pii]
AID - 10.3390/cells10113015 [doi]
PST - epublish
SO  - Cells. 2021 Nov 4;10(11):3015. doi: 10.3390/cells10113015.