PMID- 10508588
OWN - NLM
STAT- MEDLINE
DCOM- 20000104
LR  - 20190728
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 9
IP  - 17
DP  - 1999 Sep 9
TI  - Regulation of epidermal growth factor receptor traffic by the small GTPase rhoB.
PG  - 955-8
AB  - Members of the Rho family of small GTPases control cell adhesion and motility
      through dynamic regulation of the actin cytoskeleton. Although twelve family
      members have been identified, only three of these - RhoA, Rac and Cdc42 - have
      been studied in detail. RhoA regulates the formation of focal adhesions and the
      bundling of actin filaments into stress fibres. It is also involved in other cell
      signalling pathways including the regulation of gene expression and the
      generation of lipid second messengers [1] [2]. RhoA is very closely related to
      two other small GTPases about which much less is known: RhoB and RhoC (which are 
      approximately 83% identical). Perhaps the most intriguing of these is RhoB. RhoA 
      is largely cytosolic but translocates to the plasma membrane on activation. RhoB,
      however, is entirely localised to the cytosolic face of endocytic vesicles [3]
      [4]. This suggests a potential role for RhoB in regulating endocytic traffic;
      however, no evidence has been presented to support this. RhoA has been shown to
      act at the plasma membrane to regulate the clathrin-mediated internalisation of
      transferrin receptor [5] and of the muscarinic acetylcholine receptor [6]. We
      have recently demonstrated that RhoB binds the RhoA effector, PRK1 and targets it
      to the endosomal compartment [7]. We show here that RhoB acts through PRK1 to
      regulate the kinetics of epidermal growth factor receptor traffic.
FAU - Gampel, A
AU  - Gampel A
AD  - Department of Biochemistry, School of Medical Sciences University of Bristol,
      Bristol, BS8 1TD, UK.
FAU - Parker, P J
AU  - Parker PJ
FAU - Mellor, H
AU  - Mellor H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Curr Biol
JT  - Current biology : CB
JID - 9107782
RN  - 0 (Amides)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Pyridines)
RN  - 138381-45-0 (Y 27632)
RN  - EC 2.7.1.- (protein kinase N)
RN  - EC 2.7.10.1 (ErbB Receptors)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (rho-Associated Kinases)
RN  - EC 2.7.11.13 (Protein Kinase C)
RN  - EC 3.6.5.2 (rhoB GTP-Binding Protein)
SB  - IM
MH  - Amides/pharmacology
MH  - Amino Acid Substitution
MH  - Animals
MH  - Cytosol/metabolism
MH  - Endocytosis/*physiology
MH  - Enzyme Inhibitors/pharmacology
MH  - ErbB Receptors/*metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - Mice
MH  - Neoplasm Proteins/physiology
MH  - Protein Kinase C
MH  - Protein-Serine-Threonine Kinases/antagonists & inhibitors/genetics/physiology
MH  - Pyridines/pharmacology
MH  - Signal Transduction/*physiology
MH  - rho-Associated Kinases
MH  - rhoB GTP-Binding Protein/*physiology
EDAT- 1999/10/06 00:00
MHDA- 1999/10/06 00:01
CRDT- 1999/10/06 00:00
PHST- 1999/10/06 00:00 [pubmed]
PHST- 1999/10/06 00:01 [medline]
PHST- 1999/10/06 00:00 [entrez]
AID - S0960-9822(99)80422-9 [pii]
AID - 10.1016/s0960-9822(99)80422-9 [doi]
PST - ppublish
SO  - Curr Biol. 1999 Sep 9;9(17):955-8. doi: 10.1016/s0960-9822(99)80422-9.