PMID- 10531379
OWN - NLM
STAT- MEDLINE
DCOM- 19991216
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 44
DP  - 1999 Oct 29
TI  - Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3
      domain-containing proteins, endophilin I and SH3PX1.
PG  - 31693-9
AB  - Metalloprotease disintegrins (a disintegrin and metalloprotease (ADAM) and
      metalloprotease, disintegrin, cysteine-rich proteins (MDC)) are a family of
      membrane-anchored glycoproteins that function in diverse biological processes,
      including fertilization, neurogenesis, myogenesis, and ectodomain processing of
      cytokines and other proteins. The cytoplasmic domains of ADAMs often include
      putative signaling motifs, such as proline-rich SH3 ligand domains, suggesting
      that interactions with cytoplasmic proteins may affect metalloprotease
      disintegrin function. Here we report that two SH3 domain-containing proteins,
      endophilin I (SH3GL2, SH3p4) and a novel SH3 domain- and phox homology (PX)
      domain-containing protein, termed SH3PX1, can interact with the cytoplasmic
      domains of the metalloprotease disintegrins MDC9 and MDC15. These interactions
      were initially identified in a yeast two-hybrid screen and then confirmed using
      bacterial fusion proteins and co-immunoprecipitations from eukaryotic cells
      expressing both binding partners. SH3PX1 and endophilin I both preferentially
      bind the precursor but not the processed form of MDC9 and MDC15 in COS-7 cells.
      Since rat endophilin I is thought to play a role in synaptic vesicle endocytosis 
      and SH3PX1 has sequence similarity to sorting nexins in yeast, we propose that
      endophilin I and SH3PX1 may have a role in regulating the function of MDC9 and
      MDC15 by influencing their intracellular processing, transport, or final
      subcellular localization.
FAU - Howard, L
AU  - Howard L
AD  - Cellular Biochemistry Program, Sloan-Kettering Institute, Memorial
      Sloan-Kettering Cancer Center, New York, New York 10021, USA.
FAU - Nelson, K K
AU  - Nelson KK
FAU - Maciewicz, R A
AU  - Maciewicz RA
FAU - Blobel, C P
AU  - Blobel CP
LA  - eng
SI  - GENBANK/AF130979
SI  - GENBANK/AF131214
GR  - F32GM18585-02/GM/NIGMS NIH HHS/United States
GR  - P30-CA-08748/CA/NCI NIH HHS/United States
GR  - R55GM51988/GM/NIGMS NIH HHS/United States
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  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Amyloid beta-Protein Precursor)
RN  - 0 (Carrier Proteins)
RN  - 0 (Disintegrins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Protease Nexins)
RN  - 0 (Protein Precursors)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (SH3GL2 protein, human)
RN  - 0 (SNX9 protein, human)
RN  - 0 (Sh3gl2 protein, mouse)
RN  - 0 (Sorting Nexins)
RN  - 0 (Vesicular Transport Proteins)
RN  - 9DLQ4CIU6V (Proline)
RN  - EC 3.4.24.- (ADAM Proteins)
RN  - EC 3.4.24.- (ADAM15 protein, human)
RN  - EC 3.4.24.- (ADAM9 protein, human)
RN  - EC 3.4.24.- (Adam15 protein, mouse)
RN  - EC 3.4.24.- (Adam15 protein, rat)
RN  - EC 3.4.24.- (Adam9 protein, mouse)
RN  - EC 3.4.24.- (Metalloendopeptidases)
SB  - IM
MH  - ADAM Proteins
MH  - *Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Amyloid beta-Protein Precursor
MH  - Animals
MH  - COS Cells
MH  - Carrier Proteins/genetics/*metabolism
MH  - Cell Compartmentation
MH  - Cloning, Molecular
MH  - Cytoplasm/chemistry
MH  - Disintegrins/genetics/*metabolism
MH  - Eukaryotic Cells/metabolism
MH  - Humans
MH  - Membrane Proteins/genetics/*metabolism
MH  - Metalloendopeptidases/genetics/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Proline
MH  - Protease Nexins
MH  - Protein Binding
MH  - Protein Precursors/metabolism
MH  - Protein Processing, Post-Translational
MH  - Receptors, Cell Surface
MH  - Recombinant Fusion Proteins/metabolism
MH  - Sequence Analysis, DNA
MH  - Sorting Nexins
MH  - Two-Hybrid System Techniques
MH  - Vesicular Transport Proteins
MH  - *src Homology Domains
EDAT- 1999/10/26 00:00
MHDA- 1999/10/26 00:01
CRDT- 1999/10/26 00:00
PHST- 1999/10/26 00:00 [pubmed]
PHST- 1999/10/26 00:01 [medline]
PHST- 1999/10/26 00:00 [entrez]
AID - 10.1074/jbc.274.44.31693 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 29;274(44):31693-9. doi: 10.1074/jbc.274.44.31693.