PMID- 22351768
OWN - NLM
STAT- MEDLINE
DCOM- 20120606
LR  - 20211021
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 287
IP  - 15
DP  - 2012 Apr 6
TI  - RED, a spindle pole-associated protein, is required for kinetochore localization 
      of MAD1, mitotic progression, and activation of the spindle assembly checkpoint.
PG  - 11704-16
LID - 10.1074/jbc.M111.299131 [doi]
AB  - The spindle assembly checkpoint (SAC) is essential for ensuring the proper 
      attachment of kinetochores to the spindle and, thus, the precise separation of 
      paired sister chromatids during mitosis. The SAC proteins are recruited to the 
      unattached kinetochores for activation of the SAC in prometaphase. However, it 
      has been less studied whether activation of the SAC also requires the proteins 
      that do not localize to the kinetochores. Here, we show that the nuclear protein 
      RED, also called IK, a down-regulator of human leukocyte antigen (HLA) II, 
      interacts with the human SAC protein MAD1. Two RED-interacting regions identified 
      in MAD1 are from amino acid residues 301-340 and 439-480, designated as 
      MAD1(301-340) and MAD1(439-480), respectively. Our observations reveal that RED 
      is a spindle pole-associated protein that colocalizes with MAD1 at the spindle 
      poles in metaphase and anaphase. Depletion of RED can cause a shorter mitotic 
      timing, a failure in the kinetochore localization of MAD1 in prometaphase, and a 
      defect in the SAC. Furthermore, the RED-interacting peptides MAD1(301-340) and 
      MAD1(439-480), fused to enhanced green fluorescence protein, can colocalize with 
      RED at the spindle poles in prometaphase, and their expression can abrogate the 
      SAC. Taken together, we conclude that RED is required for kinetochore 
      localization of MAD1, mitotic progression, and activation of the SAC.
FAU - Yeh, Pei-Chi
AU  - Yeh PC
AD  - Institute of Medical Sciences, Tzu-Chi University, Hualien 97004, Taiwan.
FAU - Yeh, Chang-Ching
AU  - Yeh CC
FAU - Chen, Yi-Cheng
AU  - Chen YC
FAU - Juang, Yue-Li
AU  - Juang YL
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120218
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Cytokines)
RN  - 0 (IK protein, human)
RN  - 0 (MAD1L1 protein, human)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (enhanced green fluorescent protein)
RN  - 147336-22-9 (Green Fluorescent Proteins)
SB  - IM
MH  - Cell Cycle Checkpoints
MH  - Cell Cycle Proteins/*metabolism
MH  - Cytokines/genetics/metabolism/*physiology
MH  - Gene Knockdown Techniques
MH  - Green Fluorescent Proteins/metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Kinetochores/*metabolism
MH  - *M Phase Cell Cycle Checkpoints
MH  - Mitosis
MH  - Nuclear Proteins/*metabolism
MH  - Peptide Fragments/metabolism
MH  - Protein Binding
MH  - Protein Interaction Domains and Motifs
MH  - Protein Transport
MH  - RNA Interference
MH  - Recombinant Fusion Proteins/metabolism
MH  - Single-Cell Analysis
MH  - Time-Lapse Imaging
MH  - Two-Hybrid System Techniques
PMC - PMC3320919
EDAT- 2012/02/22 06:00
MHDA- 2012/06/07 06:00
PMCR- 2013/04/06
CRDT- 2012/02/22 06:00
PHST- 2012/02/22 06:00 [entrez]
PHST- 2012/02/22 06:00 [pubmed]
PHST- 2012/06/07 06:00 [medline]
PHST- 2013/04/06 00:00 [pmc-release]
AID - S0021-9258(20)53097-4 [pii]
AID - M111.299131 [pii]
AID - 10.1074/jbc.M111.299131 [doi]
PST - ppublish
SO  - J Biol Chem. 2012 Apr 6;287(15):11704-16. doi: 10.1074/jbc.M111.299131. Epub 2012 
      Feb 18.