Find protein-protein or protein-gen interaction in the following text.
Determine the interaction type if possible.
Present the found interaction partners in the following form:
partner1 ->-interaction type-> partner2 \n
partner1 and partner 2 should be as short as possible.
DO not forget the "->" and "\n" symbols for every interactions.

An example for the task is given below.
Text:
Heat shock proteins (HSPs) function as molecular chaperones and are key components responsible for protein folding, assembly, translocation, and degradation under stress conditions. However, little is known about how HSPs stabilize proteins and membranes in response to different hormonal or environmental cues in plants. Here, we combined molecular, biochemical, and genetic approaches to elucidate the involvement of cytosolic HSP70-3 in plant stress responses and the interplay between HSP70-3 and plasma membrane (PM)-localized phospholipase Dδ (PLDδ) in Arabidopsis (Arabidopsis thaliana). Analysis using pull-down, coimmunoprecipitation, and bimolecular fluorescence complementation revealed that HSP70-3 specifically interacted with PLDδ. HSP70-3 bound to microtubules, such that it stabilized cortical microtubules upon heat stress. We also showed that heat shock induced recruitment of HSP70-3 to the PM, where HSP70-3 inhibited PLDδ activity to mediate microtubule reorganization, phospholipid metabolism, and plant thermotolerance, and this process depended on the HSP70-3-PLDδ interaction. Our results suggest a model whereby the interplay between HSP70-3 and PLDδ facilitates the re-establishment of cellular homeostasis during plant responses to external stresses and reveal a regulatory mechanism in regulating membrane lipid metabolism. 
Interactions:
HSP70-3->interaction->Dδ
#Task
Text:
J-like proteins (JLPs) are emerging as ancillaries to the cellular chaperone 
network. They modulate functions of Hsp70:J-domain protein (JDP) systems in 
novel ways thereby having key roles in diverse plant processes. J-domain 
proteins (JDPs) form an obligate co-chaperone partnership with Hsp70s with their 
highly conserved J-domain to steer protein quality control processes in the 
cell. The HPD motif between helix II and helix III of the J-domain is crucial 
for JDP's interaction with Hsp70s. According to the most recent classification, 
J-like proteins (JLPs) form an extended class of the JDP family possessing a 
degenerate J-domain with the HPD motif non-conservatively replaced by other 
amino acid residues and hence are not able to interact with Hsp70s Provide your reponse without using the word translocation.
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