PMID- 26962298
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20160310
LR  - 20231111
IS  - 1389-2029 (Print)
IS  - 1875-5488 (Electronic)
IS  - 1389-2029 (Linking)
VI  - 16
IP  - 4
DP  - 2015 Aug
TI  - Role of Protein Tyrosine Phosphatases in Plants.
PG  - 224-36
LID - 10.2174/1389202916666150424234300 [doi]
AB  - Reversible protein phosphorylation is a crucial regulatory mechanism that 
      controls many biological processes in eukaryotes. In plants, phosphorylation 
      events primarily occur on serine (Ser) and threonine (Thr) residues, while in 
      certain cases, it was also discovered on tyrosine (Tyr) residues. In contrary to 
      plants, extensive reports on Tyr phosphorylation regulating a large numbers of 
      biological processes exist in animals. Despite of such prodigious function in 
      animals, Tyr phosphorylation is a least studied mechanism of protein regulation 
      in plants. Recently, various chemical analytical procedures have strengthened the 
      view that Tyr phosphorylation is equally prevalent in plants as in animals. 
      However, regardless of Tyr phosphorylation events occuring in plants, no evidence 
      could be found for the existence of gene encoding for Tyr phosphorylation i.e. 
      the typical Tyr kinases. Various methodologies have suggested that plant 
      responses to stress signals and developmental processes involved modifications in 
      protein Tyr phosphorylation. Correspondingly, various reports have established 
      the role of PTPs (Protein Tyrosine Phosphatases) in the dephosphorylation and 
      inactivation of mitogen activated protein kinases (MAPKs) hence, in the 
      regulation of MAPK signaling cascade. Besides this, many dual specificity protein 
      phosphatases (DSPs) are also known to bind starch and regulate starch metabolism 
      through reversible phosphorylation. Here, we are emphasizing the significant 
      progress on protein Tyr phosphatases to understand the role of these enzymes in 
      the regulation of post-translational modification in plant physiology and 
      development.
FAU - Shankar, Alka
AU  - Shankar A
AD  - Department of Plant Molecular Biology, University of Delhi South Campus, Benito 
      Juarez Road, Dhaula Kuan, New Delhi-110021, India.
FAU - Agrawal, Nisha
AU  - Agrawal N
AD  - Department of Plant Molecular Biology, University of Delhi South Campus, Benito 
      Juarez Road, Dhaula Kuan, New Delhi-110021, India.
FAU - Sharma, Manisha
AU  - Sharma M
AD  - Department of Plant Molecular Biology, University of Delhi South Campus, Benito 
      Juarez Road, Dhaula Kuan, New Delhi-110021, India.
FAU - Pandey, Amita
AU  - Pandey A
AD  - Department of Plant Molecular Biology, University of Delhi South Campus, Benito 
      Juarez Road, Dhaula Kuan, New Delhi-110021, India.
FAU - Girdhar K Pandey, Margarita
AU  - Girdhar K Pandey M
AD  - Department of Plant Molecular Biology, University of Delhi South Campus, Benito 
      Juarez Road, Dhaula Kuan, New Delhi-110021, India.
LA  - eng
PT  - Journal Article
PL  - United Arab Emirates
TA  - Curr Genomics
JT  - Current genomics
JID - 100960527
PMC - PMC4765517
OTO - NOTNLM
OT  - Carbohydrate binding module
OT  - Kinases
OT  - Laforin
OT  - Protein tyrosine phosphatase
OT  - Signal transduction
OT  - Stress.
OT  - Tyrosine phosphorylation
EDAT- 2016/03/11 06:00
MHDA- 2016/03/11 06:01
PMCR- 2016/02/01
CRDT- 2016/03/11 06:00
PHST- 2015/03/13 00:00 [received]
PHST- 2015/04/19 00:00 [revised]
PHST- 2015/04/24 00:00 [accepted]
PHST- 2016/03/11 06:00 [entrez]
PHST- 2016/03/11 06:00 [pubmed]
PHST- 2016/03/11 06:01 [medline]
PHST- 2016/02/01 00:00 [pmc-release]
AID - CN-16-224 [pii]
AID - 10.2174/1389202916666150424234300 [doi]
PST - ppublish
SO  - Curr Genomics. 2015 Aug;16(4):224-36. doi: 10.2174/1389202916666150424234300.