PMID- 10502414
OWN - NLM
STAT- MEDLINE
DCOM- 19991101
LR  - 20101118
IS  - 0014-4827 (Print)
IS  - 0014-4827 (Linking)
VI  - 252
IP  - 1
DP  - 1999 Oct 10
TI  - Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal
      helix-loop-helix domain.
PG  - 224-35
AB  - HEF1, p130(Cas), and Efs define a family of multidomain docking proteins which
      plays a central coordinating role for tyrosine-kinase-based signaling related to 
      cell adhesion. HEF1 function has been specifically implicated in signaling
      pathways important for cell adhesion and differentiation in lymphoid and
      epithelial cells. While the SH3 domains and SH2-binding site domains (substrate
      domains) of HEF1 family proteins are well characterized and binding partners
      known, to date the highly conserved carboxy-terminal domains of the three
      proteins have lacked functional definition. In this study, we have determined
      that the carboxy-terminal domain of HEF1 contains a divergent helix-loop-helix
      (HLH) motif. This motif mediates HEF1 homodimerization and HEF1
      heterodimerization with a recognition specificity similar to that of the
      transcriptional regulatory HLH proteins Id2, E12, and E47. We had previously
      demonstrated that the HEF1 carboxy-terminus expressed as a separate domain in
      yeast reprograms cell division patterns, inducing constitutive pseudohyphal
      growth. Here we show that pseudohyphal induction by HEF1 requires an intact HLH, 
      further supporting the idea that this motif has an effector activity for HEF1,
      and implying that HEF1 pseudohyphal activity derives in part from interactions
      with yeast helix-loop-helix proteins. These combined results provide initial
      insight into the mode of function of the HEF1 carboxy-terminal domain and suggest
      that the HEF1 protein may interact with cellular proteins which control
      differentiation.
CI  - Copyright 1999 Academic Press.
FAU - Law, S F
AU  - Law SF
AD  - Division of Basic Science, Fox Chase Cancer Center, Philadelphia, Pennsylvania
      19111, USA.
FAU - Zhang, Y Z
AU  - Zhang YZ
FAU - Fashena, S J
AU  - Fashena SJ
FAU - Toby, G
AU  - Toby G
FAU - Estojak, J
AU  - Estojak J
FAU - Golemis, E A
AU  - Golemis EA
LA  - eng
GR  - CA-06927/CA/NCI NIH HHS/United States
GR  - R01-CA63366/CA/NCI NIH HHS/United States
GR  - T32 CA09035/CA/NCI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Exp Cell Res
JT  - Experimental cell research
JID - 0373226
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (BCAR1 protein, human)
RN  - 0 (Crk-Associated Substrate Protein)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (EFS protein, human)
RN  - 0 (ID2 protein, human)
RN  - 0 (Inhibitor of Differentiation Protein 2)
RN  - 0 (NEDD9 protein, human)
RN  - 0 (Phosphoproteins)
RN  - 0 (Proteins)
RN  - 0 (Repressor Proteins)
RN  - 0 (Retinoblastoma-Like Protein p130)
RN  - 0 (TCF Transcription Factors)
RN  - 0 (TCF7L1 protein, human)
RN  - 0 (Transcription Factor 7-Like 1 Protein)
RN  - 0 (Transcription Factors)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Cell Line
MH  - Conserved Sequence
MH  - Crk-Associated Substrate Protein
MH  - DNA-Binding Proteins/chemistry/genetics
MH  - Dimerization
MH  - HeLa Cells
MH  - Helix-Loop-Helix Motifs/genetics
MH  - Humans
MH  - Inhibitor of Differentiation Protein 2
MH  - Molecular Sequence Data
MH  - Phosphoproteins/*chemistry/genetics
MH  - Point Mutation
MH  - Protein Structure, Quaternary
MH  - *Proteins
MH  - *Repressor Proteins
MH  - Retinoblastoma-Like Protein p130
MH  - Sequence Deletion
MH  - TCF Transcription Factors
MH  - Transcription Factor 7-Like 1 Protein
MH  - *Transcription Factors
EDAT- 1999/09/30 00:00
MHDA- 1999/09/30 00:01
CRDT- 1999/09/30 00:00
PHST- 1999/09/30 00:00 [pubmed]
PHST- 1999/09/30 00:01 [medline]
PHST- 1999/09/30 00:00 [entrez]
AID - 10.1006/excr.1999.4609 [doi]
AID - S0014-4827(99)94609-8 [pii]
PST - ppublish
SO  - Exp Cell Res. 1999 Oct 10;252(1):224-35. doi: 10.1006/excr.1999.4609.